DK 3876 CH 25

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CONTENTS
Chemical Measurements
Marilyn C. Erickson
Department of Food Science and Technology, University of Georgia, Grifn, Georgia, USA
I. Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . II. Evaluation of Prefreezing Treatments . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . A. Blanching . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . B. Freshness . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . C. Irradiation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . III. Methods to Assess Differentiation of Fresh from Frozen . . . . . . . . . . . . . . . . . . . . . A. Measurement of Enzyme Activity . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . B. Measurement of Volatile Composition . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . IV. Methods to Assess Nutritional Degradation during Freezing or Frozen Storage . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . A. Ascorbic Acid and Organic Acid Measurements . . . . . . . . . . . . . . . . . . . . . . . B. Glucosinolate Measurement . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . C. Folate Measurement . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . V. Methods to Assess Lipid Degradation during Freezing or Frozen Storage . . . . . . . . VI. Methods to Assess Protein Degradation during Freezing or Frozen Storage . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . VII. Methods to Assess Carbohydrate and Pigment Degradation during Freezing or Frozen Storage . . . . . . . . . . . . . . . . . . . . . . . . . . . . VIII. Chemical Measurements to Monitor Chemical and Microbial Additives/Contaminants in Frozen Foods . . . . . . . . . . . . . . . . . . . . . . . . . IX. Conclusions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
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I. INTRODUCTION
Chemicals are the building blocks of foods and hence are responsible for the physical and sensory properties of those foods. During freezing and frozen storage, chemical reactions occur; while they are slower than those occurring at higher temperatures, they often have undesirable consequences. To quantify those changes, analyses have been developed that target either substrates or products of the reactions. This chapter provides an overview of those chemical measurements that assess degradation of vitamins, lipids, proteins, carbohydrates, and pigments. This chapter presents a brief description of the methodology as well as a number of examples of studies where those measurements have been incorporated. The use of chemical measurements to differentiate fresh from frozen product is also presented.
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2006 by Taylor & Francis Group, LLC
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II. EVALUATION OF PREFREEZING TREATMENTS A. BLANCHING

Analyses to measure the application or effectiveness of prefreezing treatments are critical for maximizing quality retention in frozen products. In vegetable processing, blanching has long been used to slow quality deterioration caused by enzyme activities. Residual activity of those enzymes can therefore be used as an indicator of the adequacy of blanching. As an illustration of this relationship, blanching time was inversely related to residual peroxidase activity in frozen broccoli orets [1]. Surprisingly, only a few studies have demonstrated correlation between residual peroxidase activity and undesirable quality in frozen vegetables [2,3]; therefore, several other enzymes have been targeted as indices to blanching adequacy including lipoxygenase and cystine lyase [4 6]. Targeting either of these enzymes that are known to generate off-odors and off-avors has resulted in signicantly shorter blanch times and improved nutritional and sensory quality of frozen vegetables. The standard method for measuring lipoxygenase activity involves incubation of the sample with linoleic acid and measurement of conjugated dienes or hydroperoxides spectrophotometrically. Coupled reactions with carotenoid bleaching, however, have also been used [5]. At rst glance, such reactions suggest that bleaching of endogenous carotenoids in frozen vegetables could also be used to monitor adequacy of blanch treatments. In a recent study, however, rates of pigment decomposition varied in three cultivars of red peppers, suggesting the existence of different inherent stabilities [7].
B. FRESHNESS
Application of freezing is designed to extend product shelf-life, however, nal product quality is also based on raw material quality. For example, in the case of sh, initial quality can vary, from live to spoiled, prior to freezing. Hence, several freshness indicators have been adopted for evaluation of frozen product quality. These indicators include the high-performance liquid chromatography (HPLC) or biosensor analysis of K1 (a ratio based on the changes in the level of catabolites of adenosine triphosphate (ATP) occurring in the muscle after death) and putrescine (a biogenic amine generated via microbial metabolic processes) [8]. Putrescine, at a reject level of 3 ppm, conrmed sensory analysis decisions on frozen Penaeid shrimp of the level of decomposition that had occurred during holding prior to freezing [9]. On the basis of the observation that ATP breakdown and generation of inosine monophosphate (IMP) occurred during frozen storage, caution should be exercised with the use of nucleotide degradation as a measure of prefreezing decomposition [10]. Hypoxanthine has also been shown to increase in scallop adductor muscles during frozen storage when the product was frozen immediately after processing [11].
C. IRRADIATION
Owing to the potential for pathogen contamination and growth in products prior to freezing and the ability of these pathogens to survive freezing and frozen storage, irradiation has been proposed as an effective technology to decontaminate frozen foods. As regulations in many countries require that irradiated food be labeled as such, reliable scientic tests that can detect whether a food has been irradiated or not have been developed. Both thermoluminescence, which measures the light emitted from the inorganic components of a sample as it is rapidly heated, and electron spin resonance spectroscopy, which measures free radicals, depend on the presence of solid matrices (bone, traces of silicate minerals as surface contamination, etc.) [12,13]. Other potential markers for irradiation include long-chain hydrocarbons, 2-alkylcyclobutanones, o-tyrosine, radiolytic products of DNA, and radiolytic H2 and CO gases [14 22]. For example, based on the limit of detection for radiolytic products of 16:2, 17:1, and 17:2, an irradiation dose of 0.25 kGy could be distinguished in irradiated frozen meat and poultry [21]. Similarly, radiolytic H2 and CO have proven more useful as
Handbook of Frozen Food Processing and Packaging
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irradiation markers in frozen foods compared with unfrozen food due to lower diffusion losses during storage. Using those gases as a probe, irradiated frozen shrimp could be distinguished from nonirradiated shrimp for 3 months after 1.1 8.8 kGy irradiation. Irradiated frozen cod slices and oyster could also be distinguished for at least two months at the dose ranges of 1.4 5.5 and 1.2 6.0 kGy, respectively [18]. In the case of the DNA comet assay (a single-cell gel electrophoresis assay measuring DNA damage), however, several restrictions limit its usefulness as an irradiation marker. The DNA comet assay cannot be used with processed meats (e.g., cooked, roasted) as DNA is damaged by this treatment. Also, extensive DNA damage occurs with repeated freeze thawing. Attempts to circumvent the inuence of these other damaging factors have been made with the calculation of a relative damage index (RDI). The RDI has enabled discrimination of treatment levels within each treatment but cannot differentiate samples between treatments [22].
III. METHODS TO ASSESS DIFFERENTIATION OF FRESH FROM FROZEN

Although freezing is an excellent method to extend the storage life of foods, consumers perceive frozen product as inferior to fresh product. As a result of this, lower prices are commonly assigned to frozen foods. To prevent fraudulent sale of frozen products as fresh, methods are needed to differentiate these product forms. Hence, several approaches that target changes in chemical constituents within the product have been advocated.
A. MEASUREMENT OF ENZYME ACTIVITY

On the basis that freezing and thawing lead to cellular disruption and release of bound enzymes into the cellular uid, one approach for distinguishing fresh from frozen thawed food includes measuring the activities of several mitochondrial or lysosomal enzymes. Examples of mitochondrial enzymes include b-hydroxyacyl-CoA-dehydrogenase or HADH [23,24], L -malate-NADP-oxidoreductase [25], aspartate aminotransferase [25,26], fumarase, glutamate, or lactate dehydrogenases [27], cytochrome oxidase [28,29], and L -malate dehydrogenase [30]. Lysosomal enzymes that have been investigated include a-glucosidase [24,31 33], b-N-acetylglucosaminidase [24,31 33], acid phosphatase [31], b-galactosidase [27], and b-glucuronidase [27]. One disadvantage of a mitochondrial enzyme serving as an indicator of freezing is in the existence of corresponding isoenzymes in the cytoplasm. Therefore electrophoresis or similar separation procedures have to be applied, making it difcult to obtain quantitative results. Lysosomal enzymes, however, can be readily distinguished from cytoplasmic and bacterial enzymes by their activity in the acid pH range. In any event, before using either mitochondrial or lysosomal enzymes as markers, it is important to verify that other stresses imposed on the product do not facilitate perturbations in the enzyme activities. For example, while HADH activity was signicantly higher in frozen thawed frog legs than in unfrozen legs, HADH activity was not affected by the storage time in crushed ice up to 6 days [23]. Assays based on a-glucosidase activity, on the contrary, require that freshness measurements be conducted to avoid confusing a frozen thawed sh from a sh in an advanced stage of spoilage [24]. Applicability of a marker enzyme may also vary with the product. Although mitochondrial aspartate aminotransferase was not found in the pressed juice of unfrozen bovine muscle, its presence in unfrozen porcine muscle implies mitochondrial damage by other stresses [26]. In some cases, however, enzyme activities may provide additional information beyond differentiation of fresh and frozen product. In the case of the mitochondrial membrane-bound cytochrome oxidase, amplication in the freezing-induced activation occurred with an ice storage period prior to freezing [29]. Multiple freeze thaw cycles could also be distinguished in rainbow trout through enzyme activities of a-glucosidase and b-N-acetylglucosaminidase [32].
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B. MEASUREMENT OF VOLATILE COMPOSITION

Another group of analyses that have been used to differentiate fresh from frozen product has focused on the volatile composition of the products. Using headspace gas chromatography (GC) and electronic nose instruments, three types of commercial orange juice samples (pasteurized not from concentrate, frozen concentrate, and single strength juice reconstituted from concentrate) were evaluated. Initially 25 volatile juice constituents were screened in the GC data but through backward stepwise discriminant analysis, 11 volatiles afforded consistent separation of the orange juice into three distinct groups. In contrast, discriminant analysis of data generated with an electronic nose containing 11 sensors could not distinguish the frozen concentrated orange juice from the other two samples [34]. Ideally, methods to differentiate fresh from frozen should be rapid, nondestructive, accurate, and adaptable to online monitoring in processing plants or portable hand-held instruments in the eld. Spectroscopic techniques may be used to measure physical characteristics of frozen foods (see Chapter 24) and also be used to measure changes in one or more chemicals that occur with freezing and frozen storage. For example, near-infrared diffuse reectance spectroscopy has been used to classify samples in frozen or unfrozen beef using 400 2500 nm spectra on centrifuged meat juice [35]. Similarly, Fourier transform infrared spectral data between 1600 and 800 nm was correlated to dimethylamine (DMA) content in minced red hake and hence successfully distinguished fresh from frozen 90% of the time [36].
IV. METHODS TO ASSESS NUTRITIONAL DEGRADATION DURING FREEZING OR FROZEN STORAGE

Freezing has proven to be a suitable procedure to prolong the shelf-life of many food products. Numerous studies, however, continue to assess whether modications have occurred in the levels of endogenous components upon freezing or storage. This section reviews some of the recent studies that have examined the nutritional quality of frozen products as it relates to vitamins, phenolic acids, and glucosinolates, whereas changes associated with lipid, protein, carbohydrates, and pigments will be addressed in subsequent sections of this chapter.
A. ASCORBIC ACID AND ORGANIC ACID MEASUREMENTS

One of the major nutrients of interest in frozen produce is ascorbic acid. Following extraction, quantication of ascorbic acid is commonly accomplished through HPLC and either ultraviolet (UV), spectrouorometric, or electrochemical detection [37 39]. Using these analytical methods, ascorbic acid has been used as a marker for the evaluation of different freezing methods and prefreezing operations. For example, freezing in carbon dioxide roughly halved the ascorbic acid degradation rate in Brussel sprouts compared with conventional freezing [40]. Castro et al. [41] demonstrated that keeping the stem intact on strawberries minimized the losses of ascorbic acid during freezing. In characterizing the responses of different products to freezing and frozen storage, degradation of ascorbic acid is commonly used as an index of the relative stability of that product. To illustrate this point, no losses of ascorbic acid were observed in frozen strawberries after 2 months of frozen storage (2 208C) [42], whereas losses did occur in frozen papayas after 12 months of frozen storage (2 188C) [43] and in frozen, fresh squeezed, unpasteurized, polyethylene-bottled orange juice following a 24-month storage (2 238C) [39]. As ascorbic acid loss is encountered for many produce items, the stability of this vitamin is also commonly used to judge the suitability of varieties and ska and cultivars for freezing. In a study comparing two types of parsley (Hamburg cv. Berlin leafy type cv. Paramount), the Hamburg type was considered the better raw material for freezing, but rate of degradation was not the determining factor in that selection. More specically, ascorbic acid losses following 9 months of frozen storage (2 208C) were similar for the two types of parsley
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(35.8 37.6%); however, the Hamburg parsley had a signicantly higher content initially [44]. In contrast to this study, signicant differences in rates of ascorbic acid degradation were observed in a study comparing four raspberry cultivars. After 365 days of storage (2 208C), Rubi, Zeva, Heritage, and Autumn Bliss cultivars suffered ascorbic acid losses of 49, 47, 34, and 56%, respectively [38]. At the same time, signicant differences also occurred in degradation of ellagic acid with decreases of 19,16, 21, and 14%. In comparison, losses of ellagic acid, in the range 30 40%, were observed over 9 months of frozen storage (2 208C) for the raspberry cultivars, Ottawa and Muskoka, respectively [45]. Measurement of this acid as well as other organic acids is commonly accomplished with HPLC and UV detection [46] and is of interest for their potential antioxidant, antimicrobial, and avor-enhancing properties. For these reasons, freezing effects on the organic acid content of low-moisture Mozzarella cheese has also been examined. In this case, organic acid results demonstrated no effect of freezing on Mozzarella samples ripened after frozen storage compared with those samples ripened before freezing [47].
B. GLUCOSINOLATE MEASUREMENT
Another group of bioactive compounds whose levels have been monitored in foods during frozen storage are the glucosinolates. These secondary plant metabolites and their breakdown products are important aroma and avor compounds in Brassica vegetables. As such, their analysis requires that they be extracted prior to separation by HPLC. In a study evaluating the glucosinolate levels of the principal and secondary inuorescences of broccoli, freezing was shown to be the best preservation process [48]. For example, no signicant differences were noted in 4-methylsulnylbutyl glucosinolate content between the fresh harvested material and frozen material for the principal inuorescence. Storage at 48C, however, reduced 4-methylsulnylbutyl glucosinolate content by 31%, whereas at room temperature (208C), the reduction was 82%.
C. FOLATE MEASUREMENT
Folates may also potentially be lost during freezing and frozen storage, and thus chemical measurements may be applied for purposes of nutritional evaluation. Using the Lactobacillus casei microbiological assay, folate losses have been observed in beef liver during the rst 30 days of storage (2 208C) [49]. When HPLC was used for folate quantication, improved packaging was held responsible for the absence of folate losses in beef liver and strawberries after 6 months of frozen storage (2 188C) [50].
V. METHODS TO ASSESS LIPID DEGRADATION DURING FREEZING OR FROZEN STORAGE

Two major mechanisms contribute to the degradation of lipids during frozen storage. They are lipid hydrolysis and lipid oxidation. To assess the contribution of these activities during frozen storage, a wide range of analyses have been undertaken that encompass measurements on their substrates, catalysts, inhibitors, and products. A list of these markers and a short description of the general approaches taken to measure these constituents are provided in Tables 25.1 Table 25.4. Inherent in any of these procedures, however, is attention to sampling and preparation of the sample for analysis. Hence, sample heterogeneity must be considered as it inuences the size and number of samples drawn. Generally, to minimize heterogeneity, materials may be ground or mixed prior to removal of the sample. As the process to achieve maximum sample homogeneity may vary, Lichon and James [76] compared 12 methods of homogenization and found that cryogenic homogenization methods (cryogenic milling; top-drive macerator/dry-ice grind) effectively pulverized the sample to a small particle size facilitating milligram subsample masses to be used for analysis. In cases where the sample is too large to analyze in its entirety, however, the location
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TABLE 25.1 Description of Methodologies Used to Measure Lipid Substrates Involved in Degradative Reactions in Frozen Foods
Constituent Polyunsaturated fatty acids (PUFAs) Description of Analysis Fatty acids in a lipid extract are esteried either with sulfuric acid in methanol [37], sodium borohydride in methanol, or potassium hydroxide in methanol; once esteried, the fatty acid methyl esters (FAMEs) are injected into a gas chromatograph for separation, and detection is through a ame ionization detector Lipids are commonly extracted with a chloroform:methanol mixture; the extract is applied to a Sep-Pak cartridge, and nonpolar lipids (i.e., triacylglycerols) are eluted with chloroform whereas polar lipids (i.e., phospholipids) are eluted with methanol; subsequent to hydrolysis, triacylglycerols may be quantied by measuring the levels of glycerol spectrophotometrically, whereas phospholipids are quantied by measuring the levels of phosphate spectrophotometrically; alternatively, either fraction may be subjected to high-pressure liquid chromatography (HPLC) and evaporative scattering detection, or esteried and subjected to gas chromatography (GC) for quantication of their fatty acid methyl esters [37] From a lipid extract, the carboxylic groups of FFA are neutralized with the addition of sodium hydroxide and a change in the color of the metacresol indicator signals the end point [51]; correction must be made for the contribution of the acidic phospholipids to the percent FFA value obtained by alkalimetric titration [52,53] FFA may be separated from triacylglycerols and phospholipids using a thin-layer chromatography plate; the spot corresponding to FFA may then be scraped off, subjected to esterication conditions, and the fatty acid methyl esters subjected to gas chromatography (GC) using an internal standard and quantied [37] Cupric acetate in pyridine is added to a lipid extract suspended in benzene where it complexes with free fatty acids; the upper layer of the two-phase system is read at 715 nm [54]
Phospholipid/triacylglycerol
Free fatty acids (FFAs)a
FFAs are products of lipolysis reactions, however, they also serve as a substrate for lipid oxidative reactions.
TABLE 25.2 Description of Methodologies Used to Measure Inhibitors Involved in Degradative Reactions of Lipids in Frozen Foods
Constituent Tocopherol Description of Analysis The frozen food material is thawed and then saponied under heat with KOH; tocopherol is extracted with organic solvents from the saponied mixture; the extract sample is dried under nitrogen prior to its reconstitution in the mobile-phase solvent; both normal-phase and reverse-phase high-pressure liquid chromatography (HPLC) may be used for separation (caution: reverse phase does not separate b- and g-tocopherols); detection is mainly by uorescence or electrochemical detection [55] The sample is homogenized with sulfosalicyclic acid; after centrifugation, an aliquot of the supernatant may either be subjected to HPLC and electrochemical detection or is added to a coupled enzyme reaction system for spectrophotometric monitoring at 412 nm [56] An acidied extract is prepared from the sample and subjected to ion-pairing or reverse-phase HPLC and electrochemical detection [37,56,57] An extract from the sample is reacted with reduced glutathione and the color development is followed spectrophotometrically at 412 nm [58] Glutathione peroxidase activity may also be based on a coupled enzyme system; with glutathione reductase, the oxidation of NADPH (monitored at 340 nm) over time is monitored [59] With phosphate buffer (pH 7.5), EDTA, xanthine, cytochrome c, xanthine oxidase, and an aliquot of a sample homogenate extract, SOD activity is determined by monitoring the inhibition in the reduction of cytochrome c between reaction mixtures with and without the sample extract at 550 nm [60]
Glutathione
Ascorbic acid Glutathione peroxidase
Superoxide dismutase (SOD)
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TABLE 25.3 Description of Methodologies Used to Measure Catalysts Involved in Degradation of Lipids in Frozen Foods.
Constituent Heme proteins/ metmyoglobin Description of Analysis A supernatant fraction is obtained via centrifugation of a phosphate-buffered (pH 6.5) homogenized sample; total heme pigments are determined on this supernatant either through direct spectrophotometric measurement at 525 nm [61] or indirectly, following exposure to sodium dithionite, at 432 and 410 nm; heme content in the direct method is calculated using the molar extinction coefcient of myoglobin whereas in the indirect method, the difference in the absorbance at the two wavelengths is compared with a standard curve constructed using hemoglobin [62] The sample is homogenized prior to exposing it to acid hydrolysis conditions at elevated temperatures; the supernatant from this acidied sample is exposed to a solution of bathophenanthroline and thioglycolic acid and then held for a brief period of time; the absorbance of this mixture is read at 540 nm and compared with an iron standard curve [61] A phosphate-buffered (pH 7.0) homogenate is prepared; the supernatant recovered after centrifugation is mixed with hydrogen peroxide; catalase activity is based on the spectrophotometric decrease in hydrogen peroxide at 240 nm [59] The supernatant recovered after centrifugation of a homogenate is incubated with linoleic acid; the increase in conjugated dienes or hydroperoxides corresponds to the level of lipoxygenase activity [5] Oxidation of guaiacol by an extract of the sample is monitored for a designated period at 420 nm [6]
Non-heme iron
Catalase
Lipoxygenase
Peroxidase Lipase/phospholipase
A phosphate-buffered (pH 7.5) homogenate is prepared from the sample; after centrifugation, an aliquot of the enzyme extract is incubated with 4-methylumbelliferyl oleate as substrate; the reaction medium is incubated at 378C and uorescence periodically monitored at excitation wavelength of 355 nm and emission wavelength of 460 nm [63]
TABLE 25.4 Description of Methodologies Used to Measure Products Generated From Degradative Reactions of Lipids in Frozen Foods
Constituent Hydroperoxides Description of Analysis Both the titrimetric method (peroxide value) and the spectrophotometric method rely on the ability of the iodide ion to reduce hydroperoxides under anaerobic conditions; determination of liberated iodine is either determined by titration with thiosulfate or the absorbance (A360) of the triiodide ion is used [64] Another spectrophotometric method for hydroperoxide is based on the ability of lipid hydroperoxides to oxidize ferrous ions; following addition of xylenol orange to the system, the absorbance is measured at 560 nm that corresponds to the complex formed between xylenol orange and ferric ions [65] Near-infrared (NIR) spectroscopy is applied to lipid extracts and the absorbance at 2076 nm is attributed to the hydroxyl group of hydroperoxides [66] The spectrophotometric absorbance of a lipid extract dissolved in isooctane is read at 232 nm; CD levels are determined by applying the extinction coefcient of CD to the absorbance value [37,6768]; sensitivity of this procedure is limited as the CD absorbance appears as a rather imprecise shoulder on the strong absorption peak of the nonperoxidized fatty acid itself; by using second-derivative spectroscopy [69,70], or ultraviolet difference spectroscopy with tandem cuvettes [71], sensitivity can be increased Following distillation or aqueous acid extraction, malondialdehyde in the sample is reacted with thiobarbituric acid and the absorbance is recorded at 532 nm; addition of a chelator and an antioxidant, such as propyl gallate, to the samples before homogenization is recommended to retard further lipid oxidation [55] Volatiles may be isolated from thawed frozen foods using three main procedures: purge and trap, solid-phase microextraction (SPME), or direct sampling of headspace; the isolated volatiles are then separated on packed or capillary columns using gas chromatography (GC); packed columns offer faster run times when only a few volatiles are of concern, whereas capillary columns generate complex volatile proles [56,72,73] A thawed sample may be placed inside a chamber of an electronic nose (gas-sensor array system); either at room temperature or after a short heating time, the vapors are exposed to the sensors; output signals are generated based on the change in resistance as vapors react with the surface of the sensor; the data are subjected to chemometric and articial neural network software to generate patterns that may be associated with the extent of lipid oxidation; no published studies have been conducted to characterize the oxidative stability of frozen foods but a correlation between sensor response and oxidative stability of icestored herring has been reported [74] Lipids are extracted, typically with chloroform:methanol, and then saponied; after isolation of the nonsaponiable fraction, cholesterol oxidation products may be puried using Sep-Pak cartridges and a series of solvent mixtures with increasing polarity; the isolated fraction is nally silanized before subjecting the derivatized products to GC and ame ionization detection [75] Aqueous and organic uorescent pigments may be determined on a chloroform:methanol lipid extract; diluted samples of the aqueous and organic layers are taken and uorescence may be measured either with a uorometer (excitation and emission lters selected for wavelengths in the range 320390 and 420 500 nm, respectively) [37]) or a spectrouorometer (excitation, 367 nm; emission, 420 nm) [57]
Conjugated dienes (CD)
Thiobarbituric acid-reactive substances (TBARS) Volatiles
Cholesterol oxidation products
Fluorescent pigments
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of the subsample often inuences the outcome of the chemical measurement. In comparing caudal, ventral, and dorsal sections of frozen mackerel, Icekson et al. [77] observed that thiobarbituric acid values were higher in the caudal area than the two other areas. Moreover, when dark and light portions of frozen hake muscle were compared, a lower lipolytic activity but higher oxidative activity was observed in the dark muscle compared with light muscle [78]. Lipid degradative measurements have been incorporated into experimental studies for a variety of reasons. The studies listed in Table 25.5 may be divided into those that aim to examine the effects of raw material, diet, processing, and additives on lipid degradation during freezing and frozen storage. Typically, only one or two measurements are conducted to measure lipid degradation; however, in some studies a wide assortment of chemical measurements have been made to assist in characterizing the different pathways and stages that occurred prior to examination. For example, Erickson [67] determined that thiobarbituric acid-reactive substances (TBARS), headspace volatiles, and degradation of tocopherol could be used to differentiate oxidative stabilities of frozen bass samples during the early phases of lipid oxidation, whereas conjugated dienes, organic uorescent pigments, headspace volatiles, and degradation of tocopherol differentiated the bass during later stages of storage. Examination of frozen tilapia samples, however, did not nd tocopherol losses to be a useful measure of differentiating different strains [68]. Chemical measurements have also proven useful in dening the potential for storage temperatures to affect lipid oxidation of frozen meat. For example, Hansen et al. [87] used electron spin resonance to measure the mobility of the nitroxyl spin probes TEMPO and TEMPOL in fat and lean pork meat to gage mobility of natural constituents. In that study, the mobility of TEMPO in fat increased for temperatures above 2 608C and the mobility of TEMPOL in lean meat increased for temperatures above 2 408C. Ultimately, any benecial or negative aspects lipid degradation are judged by sensory evaluation. As constraints often exist for implementation of sensory tests, numerous studies have examined the correlation between chemical and sensory responses in an attempt to use the chemical measurements as a predictor of sensory perception. Using frozen-stored channel catsh, for example, oxidized oil avor was highly correlated to total volatile aldehydes but not individual volatiles [72]. Bak et al. [88] also found that more than one volatile was necessary to predict the score of rancid taste and rancid odor of shrimp meat. Peroxide values and free fatty acid levels were shown to be the best parameters to describe increases in train oil taste, metal taste, and bitter taste in frozen Atlantic salmon [89]. Conrmation of this association was later demonstrated upon addition of unsaturated fatty acids to fresh minced salmon [90]. Chemical measurements to measure lipid degradation often involve multiple steps and expensive instrumentation in the laboratory, however, other analyses that could be conducted online or in the eld are also being developed. For example, a portable low-resolution gas-phase Fourier transform infrared (FT-IR) analyzer was applied to the analysis of volatile compounds of thawed strawberries [91]. As no two compounds have identical IR-spectra, FT-IR is a highly characteristic measurement. Odor sensors, on the contrary, involve a more simplied approach to measure headspace volatiles. In these portable instruments, one or two metal oxide semiconductor sensor elements are used in conjunction with an internal micro air pump [92]. When one sensor element is present, the odor intensity is displayed as a numeric value. If a second element is present, information about the odor category may also be displayed. Successful application of an odor sensor has been demonstrated in an iced sh storage study [93] and thus the potential exists for this to be a valid measurement in frozen storage studies.
VI. METHODS TO ASSESS PROTEIN DEGRADATION DURING FREEZING OR FROZEN STORAGE

Another major component in frozen foods that is subject to degradation is protein. To measure this denaturation, a number of assays have been examined and these are described in Table 25.6. Some
TABLE 25.5 Selected Studies Using Measurements of Lipid Degradation

Measurements of Lipid Degradation Cholesterol Oxidation Products Heme Proteins=Metmyoglobin Phospholipids=Triacylglyerols
Polyunsaturated Fatty Acids
TBARS Malonaldehyde
Glutathione Peroxidase
Superoxide Dismutase
Lipase=Phospholipase
Fluorescent Pigments
Hydroperoxides=CD
Free Fatty Acids
Non-heme Iron
Ascorbic Acid
Glutathione
Tocopherol
Objective of Study Comparison of lipid deterioration in cod and haddock during frozen storage Lipid characterization in the scallops adductor muscle during frozen storage Characterization of antioxidant proles for channel catsh during frozen storage Effect of freezing on the activity of catalase in apple esh tissue Characterization of lipids and lipolytic activities of pig muscle during frozen storage Lipolysis and lipid oxidation in frozen minced mackerel in relation to presence of gelatin Effect of dietary a-tocopherol supplementation on cholesterol oxidation in frozen vacuum packaged, cooked beef steaks
3 3 3 3 3 3 3 3 3 3 3 3 3 3 3
[79] [80] 3 [37] [81]
3 3
3 3 3 3
[63] [82] [83]
(Table continued ) 545
References
Volatiles
Catalase
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TABLE 25.5
Continued
Measurements of Lipid Degradation Heme Proteins=Metmyoglobin Phospholipids=Triacylglyerols Cholesterol Oxidation Products
Polyunsaturated Fatty Acids
Glutathione Peroxidase
Superoxide Dismutase
Lipase=Phospholipase
TBARS Malonaldehyde
Free Fatty Acids
Ascorbic Acid
Glutathione
Tocopherol
Hydroperoxides=CD
Non-heme Iron
Fluorescent Pigments
Objective of Study Inuence of dietary fat source, and a-tocopherol, and ascorbic supplementation on lipid oxidation in frozen dark chicken meat Effect of dietary vitamin E on the oxidative stability of frozen turkey breast meat Inuence of prefreezing storage on lipid oxidation in llets of herring during frozen storage Effect of washing mackerel llets on subsequent lipid oxidation during frozen storage Lipid stability of frozen horse mackerel with brine pretreatment Effect of multiple freeze thaw cycles on lipid oxidation of catsh muscle Inuence of NaCl on antioxidant enzyme activity and lipid oxidation in frozen ground pork Effect of commercial plant extract on the stability of horse mackerel
Catalase
[84]
3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3
[85] [57] [62] [86] [61] [59] [58]
References
Volatiles
TABLE 25.6 Description of Methodologies Used to Measure Protein Degradation in Frozen Foods.
Assay or Assay Target Amino acids High-resolution nuclear magnetic resonance (NMR) spectroscopy Description of Analysis Samples are acid hydrolyzed at elevated temperatures (1108C), dried, derivatized with phenylisothiocyanate, and then subjected to HPLC [94] Water or salt extracts containing D2O are subjected to the following conditions: proton NMR spectra are run on a Fourier transform spectrometer at either 300 or 400 mHz, data points are collected with a 308 pulse, a 15 ppm spectral width and a repetition time of 3.4 s; when a large water signal is encountered, a presaturation sequence is employed, with low decoupling for 3.4 s and data collection without decoupling for 1.6 s; between 128 and 512 scans are collected as required [95] A trichloroacetic acid extract of sh muscle is reacted with a copper ammonium reagent and carbon disulde at 40508C to produce a yellow-colored copper dimethyl-dithiocarbamate; the solution is acidied with acetic acid and shaken vigorously to facilitate extraction of the colored complex into a benzene layer; after drying with sodium sulfate, absorbance of the benzene layer is measured at 440 nm [96] The majority of procedures for GC involve extraction of volatile amines from samples with trichloroacetic acid or perchloric acid, followed by neutralization of extracts; dimethylamine is then collected either by steam distillation into hydrochloric or sulfuric acid or by sampling the headspace of the neutralized extract; the isolated fraction is then injected into the GC system; alternatively, the perchloric acid extract is followed by alkalinization with 65% KOH; another extraction with toluene is performed prior to injection into the GC system [97] A trichloroacetic acid or perchloric acid extract of the sample is reacted at 608C with Nash color reagent containing acetylacetone with an excess of ammonium acetate to produce diacetyldihydrolutidine. The solution is measured spectrophotometrically at 415 nm [98] The sample is homogenized and an aliquot of the homogenate dissolved in an SDS-buffered solution; Ellmans reagent, 5,50 -dithiobis-2-nitrobenzoic acid (DTNB) and urea are then added and the absorbance is read at 412 nm; total and surface SH contents may be calculated using a molar extinction coefcient of 11,400/M cm [99]; by omitting the SDS detergent, DTNB would react only with exposed sulfhydryls instead of all sulfhydryls contained in proteins An aliquot of a sample suspension is taken and mixed with 2,4-dinitrophenylhydrazine (DNPH); after a dened period of time, trichloroacetic acid is added to the mixture to precipitate the protein; the protein pellet is washed (i.e., ethanol:ethyl acetate, 1:1) to remove unreacted DNPH before dissolving in 6.0 M guanidine hydrochloride; absorbance of the protein solution is measured at 370 nm and the protein carbonyl content calculated using a molar extinction coefcient of 22,400/M cm [99] To a sample extract containing soluble or suspended proteins, uorescence probes are added; to measure aliphatic hydrophobicity, cis-parinaric acid is added; to measure aromatic hydrophobicity, 8-anilino-1-naphthalene sulfonic acid is added; the relative uorescence intensity is plotted against protein concentration and the slope of the regression line is dened as the surface hydrophobicity
Dimethylamine
Formaldehyde
Protein sulfhydryls
Protein carbonyls
Protein hydrophobicity
547
(Table continued )
548
TABLE 25.6
Continued
Description of Analysis
Assay or Assay Target Protein solubility [100] NaCl/KCl (disrupts electrostatic bonds)
A solution of NaCl or KCl is added to a sample homogenate; the mixture is held for a dened period before it is centrifuged; the supernatant is collected for protein determination; (on occasion, the sample homogenate is centrifuged before addition of the salt solution; the supernatant from this centrifugation step is designated the water-soluble sarcoplasmic protein fraction while the precipitate is exposed to the salt solution; after centrifugation, the supernatant from this treatment regime is termed the salt-soluble protein fraction) The insoluble material from the salt extraction is treated with 2% sodium dodecyl sulfate (SDS); the supernatant recovered after centrifugation is collected for protein determination The precipitate collected from the SDS-treated sample is exposed to 2% SDS and 5% b-mercaptoethanol (b-MeOH)
SDS (disrupts noncovalent bonds) SDS plus b-MeOH (disrupts noncovalent and disulde bonds) Size-exclusion chromatography Electrophoresis
The salt-soluble protein fraction of a sample is applied to a gel column; using a ow rate of 0.5 ml/min and a buffered eluent, the protein fractions are detected with a UV detector; the molecular weights of the peaks are estimated by comparing the mobilities of the fractions to known proteins Protein fractions are solubilized in SDS and mercaptoethanol and then applied to polyacrylamide gels; following application of a electric current, the proteins are xed, then visualized primarily with Coomassie Brilliant blue; the mobility of each band is compared with the mobility of protein standards; quantitative assessment is achieved by scanning the gels on an image analyzer and relating the optical density to those of standard proteins The basis for Raman spectroscopic analysis is the inelastic scattering of photons resulting from vibrational transitions of functional groups of a molecule; both the frequency and intensity of molecular vibrations are sensitive to chemical changes and the microenvironment of functional groups, and these parameters would therefore have inuences upon the vibrational spectrum Raman spectroscopy may be applied to aqueous solutions, nonaqueous liquids, or solid systems; interference from water molecules is minimal as the water molecules exhibit weak Raman scattering, in contrast to the strong signals of water in infrared spectra; raman spectra are recorded following excitation using a laser; assignment of bands to specic vibrational modes of amino acid side chains or the polypeptide backbone is based on published data [101,102]
Raman spectroscopy
ATPase
The salt-soluble extract is diluted to give a protein concentration of approximately 25 mg/ml; in addition to a buffer (pH 7.0 7.4), the assay medium contains either CaCl2 for Ca2-ATPase, MgCl2 for Mg2-ATPase, or MgCl2 and EGTA for Mg2-EGTA-ATPase; the assay is started with the addition of ATP and terminated with trichloroacetic acid (TCA); the liberated inorganic phosphate is measured to determine the ATPase activity [99,103] To measure the level of proteolysis that has already occurred, pressed juice from the sample is prepared and TCA is added; following precipitation of the proteins, the level of nonprotein nitrogen in the supernatant is measured using either a standard protein assay (i.e. Lowry procedure) or by measuring the absorbance of the ltrate at 280 nm [104105] To measure the potential proteolytic activity, extracts are prepared and incubated with either nonspecic protein substrates (i.e., casein or hemoglobin) or substrates designed to measure specic proteases (i.e., glycyl-phenyl-alanine-2-naphthylamide for cathepsin C) [104,106,107] Myobril fragmentation index (MFI) is a useful indicator of the extent of proteolysis indicating both rupture of the I-band and breakage of intermyobril linkages; samples are homogenized, ltered to remove connective tissue, protein concentrations taken on the suspension, suspensions diluted to a nal protein concentration of 0.5 mg/ml, and then absorbance values (540 nm) multiplied by 150 to give index values for myobrillar fragmentation [108] Slices of 0.9 mm thickness are cut from the sample and warmed to room temperature (10 min) prior to running the spectra; measurements are made in the transmission mode, at a resolution of 8 cm21, using silica windows, in the spectral range of 10001876 nm (the high-absorbance water peak centered at 1927 nm limits sample thickness [109] Polyclonal antibodies to puried proteins are prepared; in the assay, puried protein is also xed to sample wells and blocked with bovine serum albumin to prevent nonspecic binding; the antibody and sample extract are added to the well and incubated for a period of time before a tracer antibody (i.e., horseradish peroxidase-IgG) is added to the system for colorimetric measurement of levels of immunological binding (as the concentration of nondenatured sample protein is increased, the probability of binding between antibody and xed protein is decreased, leading to lower levels of tracer and hence reduced color development); the levels of nondenatured protein in the sample is quantied by reference to a standard curve [110] Powdered, homogenized, or minced sample is placed in a hermetically sealed polymer-coated aluminum pan of a DSC machine while the reference pan is either empty or contains an equal weight of deionized, distilled water; samples are scanned at a designated heating rate (i.e., 108C/min) over a dened range of temperatures (i.e., 101008C); onset melting temperatures (Tm) are determined by constructing a tangent to the leading edge of a transition curve and determining the temperature at the point of intersection with the baseline; the Tm of an endothermic peak indicates the beginning of denaturation of proteins during heating; thus, the smaller the Tm, the lower the thermal stability of the protein [111 113]
Proteolysis/proteolytic activity
Fourier transform near-infrared (FTNIR) spectroscopy
Competitive-enzyme-linked immunosorbent assay (ELISA)
Differential scanning calorimetry (DSC)
549
550
of the assays focus on measuring specic constituents that may be present (i.e., formaldehyde, dimethylamine, amino acids, etc.), whereas other measurements are used to understand the interactions between proteins that contribute to their degradation (i.e., protein solubility, protein sulfhydryls, protein hydrophobicity, etc.). Examples of studies incorporating these different type measurements are given in Table 25.7 and may be divided into the following categories: fundamental studies, raw material comparison, process evaluation, additive evaluation, and predictive evaluation of chemical measurements to functional properties or sensory responses. Although the newer sophisticated analytical measurements (high-resolution nuclear magnetic resonance (NMR) spectroscopy, Raman spectroscopy, Fourier transform near-infrared (FTNIR) spectroscopy) have been incorporated into studies primarily for the fundamental characterization of protein denaturation, traditional assays to measure formaldehyde content, protein solubility, and myobrillar fragmentation are more commonly employed in applied studies. Although these latter measurements have been used for several decades, improvements in the methodology continue to be implemented. For example, Hopkins et al. [108] recommended that homogenization speeds of 15,000 rpm be applied during myobrillar fragmentation assays. Moreover, in measurements of formaldehyde, Bechmann [125] demonstrated that the amount of free plus reversibly bound formaldehyde could be predicted by a linear model that was based on levels of free formaldehyde, and these values were similar to those obtained through distillation.
VII. METHODS TO ASSESS CARBOHYDRATE AND PIGMENT DEGRADATION DURING FREEZING OR FROZEN STORAGE
Although the majority of studies examining the effects of freezing and frozen storage target lipid and protein constituents, carbohydrate moieties within frozen foods may also be modied. Hence, assays to measure cell wall polysaccharide composition have shown losses in total sugars of frozen muskmelons [126]. In contrast, little change was noted in pectic substances for frozen persimmon fruit and astringency reduction was attributed to tannin insolubilization [127]. Chemical measurements for pigment degradation are another area of investigation in frozen shelf-life studies. Examples where chlorophyll measurement has been undertaken include studies on apple fruit [128], asparagus spears [129], and stir-fried pea pods [130]. Similarly, carotenoid (astaxanthin, canthaxanthin) assays have been conducted in frozen salmon [131] and rainbow trout [132], whereas heme pigment (myoglobin, oxymyoglobin, metmyoglobin) assays have been conducted in frozen beef [133], ground pork [134], and bluen tuna [135]. The development of white spots in shrimp, however, required that the constituents responsible for the quality defect rst be characterized and identied before they could routinely be monitored. Consequently, IR and Raman spectroscopy determined that the white spots were crystals of calcite and vaterite, two forms of calcium carbonate, in a matrix of chitin [136].
VIII. CHEMICAL MEASUREMENTS TO MONITOR CHEMICAL AND MICROBIAL ADDITIVES/CONTAMINANTS IN FROZEN FOODS
Studies to measure chemical migration from food contact materials to frozen foods has been limited despite test conditions being specied for frozen foods in European directives [137]. In particular, migration of adhesives and substances used in inks are relevant targets. To detect benzophenone (a photoinitiator for UV-cured ink) in frozen retail foods (Cornish pies, breaded sh sticks, potato wafes, cheese, and onion sticks), the samples were extracted with solvent, subjected to size exclusion chromatographic clean-up, and then analyzed for the targeted substance by gas chromatography mass spectrometry [138]. Similar type analyses were applied to detect model ink components (chlorodecane, butyl benzoate, dimethyl phthalate, benzophenone, and benzybutyl phthalate) in potato chips and hamburgers stored for 1 year at 2 208C.
TABLE 25.7 Selected Studies Incorporating Protein Degradation Measurements

Measurements of Protein Degradation Protein Surface Hydrophobicity Size-Exclusion Chromatography
Proteolysis=Calpain Activity
Raman Spectroscopy
NMR Spectroscopy
Protein Sulfhydryls
Protein Carbonyls
Protein Solubility
Dimethylamine
Myosin ATPase
Electrophoresis
Formaldehyde
Amino Acids
FTNIR Spectroscopy
Objective of Study Freeze denaturation of carp myobrils compared with thermal denaturation Characteristics of the salt-soluble fraction of frozen hake llets Characterization of proteins during frozen storage of minced cod Response of cod myosin to frozen storage or modication with formaldehyde Response of cod proteins to a nonenzymic free-radical-generating system during frozen storage Characterization of proteins during frozen storage of hake Characterization of proteins during frozen storage of minced red hake Characterization of water-soluble metabolites in cod and haddock subjected to frozen storage Myosin denaturation during frozen storage monitored by ELISA Modication in proteolysis of cheese subjected to frozen storage Depolymerization and aggregation of glutenin in bread dough during frozen storage Off-avor production in frozen strawberries
3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3 3
3 3 3
[114] [115] [116] [101] [117] [102] [36] [95] 3 3 [110] [107] [118] [119]
3 3
References
ELISA
DSC
551
(Table continued )
552
TABLE 25.7
Continued
Measurements of Protein Degradation Protein Surface Hydrophobicity Size-Exclusion Chromatography
Proteolysis=Calpain Activity
Raman Spectroscopy
NMR Spectroscopy
Protein Sulfhydryls
Protein Carbonyls
Protein Solubility
Dimethylamine
Electrophoresis
Myosin ATPase
Formaldehyde
Amino Acids
FTNIR Spectroscopy
Objective of Study Comparison of protein denaturation in frozen cod and haddock Variation of protein denaturation during frozen storage with lamb genotype Calpain activity in thawed rigor muscle and association with toughness Response of cod muscle proteins to different freeze thaw cycles Modication in type of aggregation as affected by frozen storage temperature Protein quality of sardine llets as affected by slow and quick defrosting Effect of pressure shift freezing and air-blast freezing on protein denaturation of frozen turbot Protein denaturation in frozen-stored minced blue whiting muscle as affected by cryostabilizers Effect of additives on protein denaturation in frozen hake muscle Effect of cryoprotectants on protein denaturation in frozen rainbow trout llets Chemical stability of antioxidant-washed beef heart surimi Relationship of foaming capacity to protein degradation of sh minces during frozen storage
3 3 3 3 3
[94] [120] [106] [61] [121] [122]
3 3 3 3
3 3 3 3
3 3
3 3 3 3 3
[123] [109] [100] [113] [99] [124]
3 3 3
References
ELISA
DSC
3 3 3 3 3
3 3
553
In frozen dough, the viability of yeast additives is critical for proper functioning. To assess this viability, various measurements have been applied to assess gas production and leachate composition of frozen yeast [139]. In the case of gassing power, previously frozen yeast is suspended in a media conducive for fermentation. The CO2 is collected over a period of time in a gas dispersion tube containing NaOH and quantied by back-titrating with HCl. In the case of leachate composition, compressed frozen thawed yeast is suspended in water, shaken for a period of time, and nitrogen and total reducing substances determined on the supernatant.
IX. CONCLUSIONS
A wide range of chemical measurements are available to measure constituents of frozen foods. Some analyses seek to measure the loss of a component, whereas others target the products of a chemical reaction. Selection of a chemical measurement is dependent on the objective of a study. In applied studies, one or more standard measurements (i.e., TBARS, dimethylamine) may be applied, whereas analyses required for fundamental studies often involve more sophisticated instrumentation (i.e., Raman spectroscopy, high-resolution NMR spectroscopy). Ultimately, the merit of a measurement should be based on its relationship to the sensory response of the product.
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25

II. EVALUATION OF PREFREEZING TREATMENTS A. BLANCHING

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

III. METHODS TO ASSESS DIFFERENTIATION OF FRESH FROM FROZEN

A. MEASUREMENT OF ENZYME ACTIVITY

2006 by Taylor & Francis Group, LLC

B. MEASUREMENT OF VOLATILE COMPOSITION

IV. METHODS TO ASSESS NUTRITIONAL DEGRADATION DURING FREEZING OR FROZEN STORAGE

A. ASCORBIC ACID AND ORGANIC ACID MEASUREMENTS

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

V. METHODS TO ASSESS LIPID DEGRADATION DURING FREEZING OR FROZEN STORAGE

2006 by Taylor & Francis Group, LLC

Free fatty acids (FFAs)a

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

Ascorbic acid Glutathione peroxidase

Superoxide dismutase (SOD)

2006 by Taylor & Francis Group, LLC

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

Conjugated dienes (CD)

Thiobarbituric acid-reactive substances (TBARS) Volatiles

Cholesterol oxidation products

2006 by Taylor & Francis Group, LLC

VI. METHODS TO ASSESS PROTEIN DEGRADATION DURING FREEZING OR FROZEN STORAGE

Handbook of Frozen Food Processing and Packaging

TABLE 25.5 Selected Studies Using Measurements of Lipid Degradation

Polyunsaturated Fatty Acids

Free Fatty Acids

[79] [80] 3 [37] [81]

[63] [82] [83]

(Table continued ) 545

2006 by Taylor & Francis Group, LLC

Polyunsaturated Fatty Acids

Free Fatty Acids

[85] [57] [62] [86] [61] [59] [58]

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

Fourier transform near-infrared (FTNIR) spectroscopy

Competitive-enzyme-linked immunosorbent assay (ELISA)

Differential scanning calorimetry (DSC)

2006 by Taylor & Francis Group, LLC

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

TABLE 25.7 Selected Studies Incorporating Protein Degradation Measurements

[94] [120] [106] [61] [121] [122]

[123] [109] [100] [113] [99] [124]

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

2006 by Taylor & Francis Group, LLC

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

2006 by Taylor & Francis Group, LLC

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

2006 by Taylor & Francis Group, LLC

2006 by Taylor & Francis Group, LLC

Handbook of Frozen Food Processing and Packaging

2006 by Taylor & Francis Group, LLC