Effect of Sodium Chloride and Phosphates on the Thermal Properties of Chicken Meat Proteins

J.M. KIJOWSKI and M.G. MAST

ABSTRACT
Maximum thermal transition (T,,) and denaturation enthalpy (AH) of water-washedmyofibrils and finely cut chicken breast muscle, treated with l-4% NaCl and/or 0.25-l% of either pyrophosphate (PP) or tripolyphosphate (TPP), were monitored by differential scanning calorimetry. Increasing the concentration of NaCl destabilized the heat resistance of the proteins in water-washed myofibrils and in meat specimens. Actin showed the greatest reduction of T,,, a 16C decline in the presence of 4% NaCl. In a meat system, the addition of 4% NaCl resulted in one T,,,, instead of five transitions, as seen in untreated meat. The presence of PP and TPP, especially in concentrations of 0.25 and 0.50%, enhanced the thermal stability of myosin. Changes in denaturation temperatures of proteins were accompanied by corresponding changes in AH.

INTRODUCTION HEATING POULTRY MEAT is accompanied changes by in appearance, flavor, texture and nutritive value. Most of the major changes which occur in meat during heating,such as shrinkage toughening tissue, release juice and disand of of coloration,arecaused alterations the muscleproteins.In by in a previousstudy by Kijowski and Mast (1988), differential scanning calorimetry(DSC) was usedto identify thermalbehaviorof intacttissues isolated and proteinfractionsof chicken broilers. The breastmuscleexhibiteda complexthermogram
with five endothermic transitions at about 57C, 62C, 67C,

changes the DSC profile of muscledenaturation in (Oreshkin et al., 1986); insteadof three endothermic transitions,four temperature maximaweremonitored. changes beefmeat The of proteinsduring frozen storageand the influenceof freezing ratewere investigated DSC by WagnerandAnon (1985). with Studieson the relationship betweenthe denaturation indiof vidual muscleproteinsandthe texturechanges meatcaused of by cookingwereconducted usingDSC by Martens al. (1982) et and Findlay et al. (1986). Thermal transitionsof myofibril systems from fish were shiftedto lower temperatures the with additionof NaCl (Wu et al., 1985). A study of the thermaldenaturation rabbit myosin in a of low ionic buffer systemwith ortho-, pyro- and tripolyphosphates concentrations 0.5% was conducted Wright and at of by Wilding (1984).A similarinvestigation the effectof various on saltson the heatstability of beef actinwas doneby Stabursvik and Martens(1980). The objectivesof this study were to evaluatethe effect of NaCl or phosphates, combinations these,on the denaand of turationtemperature (T,,) andenthalpyof denaturation (AH) of water-washed myofibrils andbroiler breastmeatproteins. MATERIALS & METHODS
Samples Seven-week-old chicken broilers were slaughtered at The Pennsylvania State University Poultry Research Farm. Birds were scalded, defeathered, eviscerated and chilled overnight in ice water. Breast muscles were removed from carcasses24 hr post-slaughter and macerated for 2 min in a Waring Commercial Food Processor. Water-washed myofibrils were obtained from breast muscle aged 24 hr, according to the procedure of Wang (1982), in which distilled water was used instead of a buffer. Preparation was carried out in a cold room (4C). Breast muscles were cut into small pieces (- 1 cm3) and weighed. Water (8 mL/g wet muscle) was added and the muscle tissue was ground in a multispeed Waring Blendor (set on blend) for three 15 set bursts at 1 min intervals. The homogenate was placed into polycarbonate bottles and centrifuged at 1880x g for 15 min in a Beckman 52-21 centrifuge. The supernatant was decanted and the pellet was thoroughly resuspended in a minimum volume of water. White connective tissuewas removed by pouring the suspensionthrough a 30-mesh strainer (Newark Wire Cloth Co., Newark, NJ) into a beaker, then increasing the total volume of water to eight times the muscle weight. The washing step was repeated four more times. The final centrifugation was done at 3840x g. Additives The following additives were incorporatedinto both the water-washed myofibrils and the ground meat: NaCl (Fisher Scientific), food grade sodium pyrophosphate, Na4P20,, and sodium tripolyphosphate, Na,P130,,, (FMC Corporation, Philadelphia). Additives were initially dissolved in 40C water; these solutions were mixed with the ground meat in an amount equal to 10% of specimen weight, and allowed to equilibrate for 12 hr at 4C. The variations of the applied additives and their amounts were: NaCl at 1, 2, 3, or 4%, pyrophosphate (PP) at 0.25,0.50,0.75, or 1%; and tripolyphosphate (TPP) at 0.25,0.50, 0.75, or 1%. In addition, the following combinations of additives were used: 2% NaCl plus 0.25% or 0.50% PP, and 2% NaCl plus 0.25% or 0.50% TPP. DSC was performed on a Perkin Elmer DSC-4. Samples (lo-15 mg) of water-washed myofibrils or finely ground meat were accurately OF FOOD SCIENCE-367

73C, and 78C at a heatingrate of 10Clmin.Water-washed myofibrils displayedtwo major transformations 55C and at 78C, which correspond myosinand actin. to In the processing poultry meat, sodium pyrophosphate of andtripolyphosphate widely usedto promote are waterbinding and reducecooking losses.The use of phosphates meat in productshas increased a result of pressure as from consumer groupsto reducesodiumlevels in food (Trout and Schmidt, 1983).The simultaneous additionof NaCl and phosphates to the meatcauses considerable modificationof physicomechanical featuresof myofibrillar proteins,the fraction mainly responsiblefor meat functionality. The combined effect of phosphates NaCl is not clearly understood. and The partial replacement NaCl by phosphate beenshownto be funcof has tionally effectivein red meat (Pepper Schmidt, 1975). and Recentlythe DSC technique beenappliedto study the has effect of a variety of processing stepson the thermalbehavior of red meat and seafood.Quinn et al. (1980) used DSC to monitorthe heatstability of beefproteinsduringprocessing of meat into sausages. authorsconcludedthat neither meThe chanicalwork donenor the presence fat affectedthe strucof tural stability of the proteins,but the presence NaCl altered of the stability, causinga reductionin the denaturation temperature. Prolonged pressure treatment muscleat about150MPa of resultedin eliminationof the thermaltransitionattributable to actin (MacFarlane al., 1981).Heatingof curedbeef caused et
Author Mast is with the Dept. of Food Science, The Pennsylvania State Univ., University Park, PA 16802. Author Kijowski s present address is Dept. of Food Technology, Agricultural Univ. of Pozan, UI. Wojska Polskiego 31, Pozan 60-624, Poland.

Volume 53, No. 2, 1988-JOURNAL

DSC OF CHICKEN TISSUE PROTEINS. . . weighed aluminum (PerkinElmerNo. 219-0062) then in pans and
sealed with a crimper. Distilled water was used as a reference sample. Two standards were used for temperature and enthalpy calibration: gallium (T=29.8C, AH=80.22 J/g) and indium (T=156.6C, AH = 28.46 J/g). The heating conditions of samples were programmed and fully controlled by a microcomputer within the DSC over the range of 20-90C; heating rate (HR) was set for all samples at WC/ min. A minimum of four replicates was used. Plots of heat flow versus temperature were obtained for each specimen and analyzed. The partial areas program of the Perkin Elmer Thermal Analysis Data Station (TADS) was used to obtain temperatures of extrapolated onset of transition (I temperature of maximum transformation or denatura,), tion (Tmar), and enthalpy of transition (AH). Thermal profiles were normalized to equal weights of the samples (10 mg) to permit comparison. Enthalpy was expressed in Joules per g protein and tempreaturein degrees Celsius. Protein analyses were performed by the macro-Kjeldahl procedure using a Kjeltec I system (Tecator, Inc., Herndon, VA). A factor of 6.25 was used to convert nitrogen to protein. models (GLM) procedure (SAS, 1985).

Dataweresubjected analysis variance, to of usingthegeneral linear

66.6a

RESULTS & DISCUSSION THERMAL TRANSITIONS of water-washed myofibrils, with increasinglevels of sodium chloride, are shown in Fig. 1. As the level of NaCl increased,decreases were observedfor the transition temperatures myosin and actin. Previousstudies of of Kijowski and Mast (1988) indicatedthat water-washed myofibrils displayed two main transitions, myosin at 57C and actin at 78C. The denaturation temperature actinwas 16.7C of lower in samples treatedwith 4% NaCl than in control samples with no NaCl. Changes myosinwere smaller,but still about for 5C lower in samplestreatedwith 4% NaCl. Simultaneously, increasesin NaCl concentrationproducedreductionsin total enthalpy. Similar resultswere found with chickenbreastmuscletreated with NaCl (Fig. 2). The top thermalcurve in Fig. 2 showsthe transitions of untreated, intact breast muscle. According to previous results (Kijowski and Mast, 1988), the first peak of the muscle thermalprofile corresponds myosin, the second to

40

50

60

70

80

SO

TEMPERATURE C Fig. 2-Thermal transitions of chicken breast muscle treated with NaCI. Means for the first peak, second peak, or &-/, respectively, which are followed by different letters, are significantly different (P < 0.05J.

I
t Control

0.25

mJ/sec.

80.7a

56.6b

553c

67.7~

14%Nsyi,

40

50

60 70 80 TEMPERATURE C

SO

Fig. l- Thermal transitions of water-washed myofibrils treated with NaCI. Means for the first peak, second peak, or AH, respectively, which are followed by different letters, are significantly different (P < 0.05). 3684OURNAL OF FOOD SCIENCE-Volume 53, No. 2, 1988

and third to sarcoplasma the last one to actin. The collagen and content of chicken breastmusclewas low; collagenprobably contributedto the third peak in the thermogramto a limited extent. The reductionin the heat stability of myosin, and particularly actin, was observedwhen muscle was treatedwith NaCl. At the same time a significant (p <: 0.05) decrease occurredin total AH. This was mainly due to decreases the in peak areasof actin and myosin. The peaksbetween63-68C, which corresponded sarcoplasma, with graduallybecame larger, and at concentrations 4% NaCl, the typical five peak tranof sition profile was severely contractedto one major transformation at 66.6C. This temperature approaches temperature the to which poultry frankfurters and other poultry products are heated(68-71C)in industrial practice. Salt can decrease the heat stability of the muscleproteins, so that they denatureand coagulateat lower processingtemperatures. The destabilizingeffect of some ions on myofibrillar proteinswas observed otherstudies in with purifiedporteins(Wright et al., 1977; Stabursvickand Martens, 1980). Quinn et al. (1980) concludedfrom their study on beef muscle and meat emulsionsthat the presence NaCl ions dramaticallyaltered of the stability by lowering the temperature denaturation. of This effect was partially reversedafter dialysis of the ground salted meat. Sodiumchloride and magnesium chloride, at concentrations up to 0.2M, also causeddecreases both denaturation in temperatureand enthalpy of collagen; the decreasewas inversely relatedto the concentration thesesalts (Lim, 1976). of At concentrationsabove 0.2M the denaturationtemperature and enthalpywere observedto increase. In contrast,NaCl ions increasethe stability of soy proteins (Hermansson,1978) and fababeanproteins (Arntfield et al., 1986). Fababean proteins,vicilin and legumin,were stabilized by NaCl up to a 4 M concentration.The stabilization effect was relatedto electrostaticinteractionand preferentialhydration. When whole breastmuscleswere finely comminutedduring preparationof myofibrils, the total enthalpy of thermal transition was reduced(p < 0.05) by about 30% from the native breastmuscle from (16.4 J/g) to the finely comminutedfrom (11.1 J/g). Although no specific information was found in the

0.25

mJ/sec.

Actin

Control

40

50

60

70

80

90

TEMPERATUREC
Fig. 3Thermal transitions of water-washed myofibrils treated

with pyrophosphate (Pf),

literaturepertainingto theseresults, Quinn et al. (1980) reportedthat mechanical work did not affect the heatstability of the protein structurein meat emulsions.However, theseauthorsbased their conclusions transitiontemperature on changes and not on enthalpy.In the presentstudy transitiontemperatures also remainedunchanged first and secondthermal (see curvesin Fig. 2). A comparison the profilesof breastmuscle of and finely comminuted breastmuscle(Fig. 2) showsthat the primarydifferenceis the reductionin peaksizefor myosinand actin. The resultsof thesephenomena not clear; they may are relateto the heatconductivitychanges to differences the or in macrostructure the myofibrils. of Values for thermal transitionsand AH for all phosphate treatmentsare presented Table 1. The influence of pyroin phosphate concentration (0.25-1.0%) on the thermalprofiles of myofibrils is presented Fig. 3. The thermal curves for in myofibrils treatedwith comparable levels of tripolyphosphate were very similar and are not displayedhere. The additionof phosphate stabilized myosin, i.e., thermal denaturation occurred at higher (~~0.05) temperatures than in the control samples. additionof 0.25 or 0.50% PP or TPP caused The the greatest stabilization.Phosphates, however,destabilized actin, i.e., as the concentration increased, denaturation was the temperaturedecreased. total enthalpyincreased The with the addition of 0.25% phosphate;adding more phosphate not did
Table I -Major thermal treated with ohosohates Type of phosphate Pyrophosphate transition temperatures iT7, T2, T3) and total enthalpy Myofibrils % 0 0.25 0.50 0.75 1.00 0 0.25 0.50 0.75 1.00 (m:bsin) 58.4d 62.9a 60.8b 59.8c 59.3c 58.4~ 61.2a 61.3a 59.7b 59.313 T2 (actin) 80.7a 78.4b 74.5c 70.9d 70.6d 80.7a 78.56 76.0~ 71.8d 71.2e

further increaseAH. The oppositeeffects of phosphates on myosin and actin are not easy to explain. From experiments dealingwith the effect of various salts on purified actin stability, Stabursvikand Martens(1980) concludedthat the stabilizing effect of KH,PO, may be, in part, an indirect result of the removalof somedestabilizingfactor, i.e., chlorideor calcium ions, during the extractionprocedure.However, in this study, PP and TPP had a destabilizingeffect on myofibrillar and chickenmeat specimens. Wright andWilding (1984)indicateda destabilization effect of pyrophosphate mg/mL protein)in experiments pur(5 with ified myosin in a buffer system(0.04M KCl, 0.5 mM DlT, 100 mM maleate,pH 6.5); similar, but smallereffects were observed ortho-andtripolyphosphates. with However,it seems logical that PP and TPP shouldcausesimilar effects, because it is known that TPP is rapidly hydrolyzedin muscleto PP. In meat samples treatedwith PP, significantheat stabilization of myosinwas observed (Table 1); simultaneously inan crease enthalpyof denaturation in occurred.This increase was greatestwith concentrations 0.25 and 0.50% phosphates. of The samesamplesshowedreducedthermalstability of actin. The actin peak was greatly diminishedwhen the PP concentration increased 0.75-1.0% (Fig. 4). Analogouschanges to were observed when TPP was addedto chickenmeat (Table 1). Phosphates affected sarcoplasmic also proteins (peaks2 and3); as the concentration phosphates increased of was (Fig. 4), peak2 increased size and peak3 decreased. in In the presence phosphates or TPP) andNaCl, waterof (PP washedmyofibrils displayed significant(p < 0.05) declinesin heat denaturation temperatures myosin and actin (Fig. 5). of A 13Cdeclinein the denaturation temperature actin and a of 2-3Cdeclinein the denaturation temperature myosinwere of observed whenNaCl and0.25%or 0.5% phosphate added were to myofibrils. A reductionin the thermalstability of both major proteinsin the presence TPP was similar. The AH of denof aturationremained same(p > 0.05).for controlsamples the and treatments containingphosphates NaCl. and In the meatsamples treatedwith NaCl and phosphates, the denaturation temperature actin was reduced 5-6C (Fig. of by 6). Increasingthe concentration phosphate of beyond0.25% did not further reduce(p > 0.05) the denaturation temperature of actin. The denaturation temperature myosin decreased of 1.5-3.oC in the presence NaCl and phosphates. midof The sectionof the thermalcurve showedonly one dominantpeak, with a maximumtemperature transformation about66C, of at insteadof the two peakstypical of sarcoplasma. This behavioris similar to that of musclesin presence of only NaCl (Fig. 2). Alterationsin the proteinsof meat were dominated the presence NaCl morethanphosphates. by of The AH of myofibrils treatedwith 2% NaCl and phosphates remainedunchanged > 0.05); however,the AH of breastmus(p cle treated with 2% NaCl andphosphates lower (p c 0.05) was than in untreated samples. The interactionsof ions with proteinsaffectedthe temperof transition (AH) of water washed myofibrils and chicken breast muscle

Breast muscle

AH
11.7b 13.9a 13.4a 13.4a 13.6a 11.7bc 12.2b 13.4a 10.9c 8.5d

(pe2
58.7~ 58.6~ 59.9b 59.913 60.6a 58.7ab 59.lab 58.4b 59.6a 59.4a

1)

(P%k:T3) 87.6a 62.5~ 62.9c 64.7b 65.3b 67.6a 63.4~ 64.2bc 64.7b 65.3b

(P2

5,

AH
ll.lb 13.4a 14.2a 12.5ab 13.0a ll.lb 13.6a 12.5ab 12.lab 12.3ab

78.6a 77.5a 77.7a 75.5b 74.3b 78.6a 77.3a 77.5a 75.0b 75.0b

Tripolyphosphate

a Mean of four replicates; means in the same columns for each phosphate having the same letter are not significantly different (p > 0.05)

Volume53, No. 2, 1988-JOURNAL

OF FOOD SCIENCE-369

DSC OF CHICKEN TISSUE PROTEINS. . .

I
4

I
II

0.25

mdlsec.

58.9a

68.7

78.7a

breast

muscle

0.25%-

8
8 5 0.75% PP ___/ ---1.0% PP
I

2% NaCl+ 0.50% PP

n
I I 1 I I

2% NaCl + 0.50% TPP

40

50

60

70

80 breast

90 muscle treated

40

50

60

70

80

90

TEMPERATURE C Fig. 4-Thermal transitions with pyrophosphate (PP). of chicken

TEMPERATURE C Fig. 6-Thermal transitions of chicken breast muscle treated with NaCl, pyrophosphate (PP) and tripolyphosphate (TPP). Means for peaks 7, 2, or 3, and AH, respectively, which are followed by different letters, are significantly different (P < 0.05).

59.2a

81.7a

68:8b

57;l b

40

50

60

70

80

90

TEMPERATURE C Fig. 5-Thermal transitions of water- washed myofibrils treated with NaCI, pyrophosphate (PP) and tripolyphosphate (TPP). Means for the first peak, second peak, or AH, respectively, which are followed by different letters, are significantly different (P < 0.05).

protein structures.Thus, there is presumablycompetitionbetweenwater moleculesand addedneutralsaltsfor the potential binding sites; the effect is that temperature,as well as energy of denaturation,is lower. An interestingobservationof this studywas that the thermal stabilizationof myosin and destabilizationof the rest of proteins in the presenceof phosphates occurredsimultaneously. This effect was the most distinct at the 0.25% and 0.50% concentrationof PP or TPP. Phosphates interact electrostatically (nonspecifically)with chargedprotein moleculesin muscle like neutralsalts.However,phosphates reactspecifically also with myosin on the sameactive binding sitesof a moleculeas thosewhich react with actin (Kiely and Martonosi, 1968) or ATF (Blum, 1960). Presumablythe site-specificreaction of PP with myosin may be linked to the stabilizing effect on this protein. The amount of specifically reacting pyro- or tripolyphosphate probably restrictedto the number of available was binding sites on the myosin head, usually reactingwith actin. At phosphate concentrations grCater OS%, the excessions than reactednonspecificallywith myosin molecules,i.e., with oppositely chargedgroups of this protein. The result was a decreasein thermal stabilization. An importantobservation the poultry processing for industry is that in chickenmuscleproductswhich incorporatesalts, the requiredfinal temperature could be lower than in productswith no salts or restricted amountsof salts. This is important regarding the quality of the final product as well as the potential for energyconservation.
REFERENCES
Arntfield, SD., Murray, E.D., and Ismond, M.A.H. 1986. Effect of salt on the thermal stability of storage proteins from fababean (Vicia fabia). J. Food Sci. 51: 371. Blum, J.H. 1960. Interaction between myosin and its substrate. Arch. Biochem. Bio hys. 87: 104. Findlay, C.J., 8 tanley, D.W., and Gullet&, A. 1986. Thermomechanical properties of beef muscle. Meat Sci. 16: 57. Hermansson, A.M. 1978. Physico- chemical aspects of soy structure formation. J. Text. Stud. 9: 33. Kiely, B. and Martonosi, A. 1968. Kinetics and substrate binding of myosin adenosine triphosphatase. J. Biol. Chem. 243: 2273.
-Continued on page 387

atureand enthalpyof denaturation.In this study, it was shown that the binding of strongly negative polyvalent anions like pyrophosphate tripolyphosphate myofibrillar protein and or by meat systemsprovided stability to myosin. The effect of ions on the thermalpropertiesof muscleproteinsmay be explained in the following manner,accordingto the suggestions Von of Hippel and Wong (1965): anion binding (in this study the chloride ions in NaCl) to potentially active sites on a protein, causesdisplacementof the water moleculeswhich stabilize
3704OURNAL OF FOOD SCIENCE-Volume 53, No. 2, 1988

even after S. UU~~U..T countswere high enoughfor detectcell able enterotoxinto have been produced.The results obtained in this study of nitrite-free bacon-like product are in general agreement reportsin the literatureon othermeatproducts. with Odor and appearance becameunacceptable most quickly in air-permeable packages,followed by N,-flushed and vacuum packages. Temperature influencedsensoryevaluation with odor and appearance degradingmore quickly at 26C than 12C, and more quickly at 12C than at 8C. Simard et al. (1985) reportedthe microflora and sensoryanalyses fresh vacuumof or nitrogen-packed beef to be significantly affected by temperatureand storagetime. Despite the influence of temperature, Nz packaging significantlyimprovedshelf life by retarding discolorationand minimizing exudate.In this study, the meat maintainedan acceptableappearance longer in vacuum and, to a lesserdegree,in nitrogen packagingwhile odor became unacceptable earlrer. The product was rejectedoutright prior to the detectionof toxin in air permeable packages. A staphylococcal hazarddeveloped 26Cin air-permeable at wrap; however, the quality attributesof appearance odor and were sufficient to deter consumption.Enterotoxin formation was preventedin air-permeable packagesat 8C and 12C in this study, but the literatureindicatesthat temperature aloneis not a reliablemeansof control. Vacuum-andN,-flushed packaging proved a deterrentto the production of staphylococcal enterotoxindespitestorageat severelyabusivetemperatures. The growth of large numbersof cells under anaerobicconditions, however, is of some concern and the mechanismby which enterotoxinproduction is inhibited requiresfurther investigation if Nz- flushed and vacuum packagingare to be effectively utilized in the preventionof staphylococcal enterotoxin formation. REFERENCES
AOAC. 1980. Official Methods of Analysis, 13th ed. Association of Official Analytical Chemists, Washington, DC. Barber, L.E. and Deibel, R.H. 1972. Effect of pH and oxygen tension on staphylococcaI growth and enterotoxin formation in fermented sausage. al. Mmrobiol. 24: 891. , J. and Townsend, N.E. 1978. Cured meats. Ch. 10. In The Science of Meat and Meat Products, J.F. Price and B.S. Schweiger (Ed.), p. 452. Food and Nutrition Press, Wes Buchanan R E and Solber gen andpH oh growth of Ca~tehni, A.G. and Niven, C.J., Jr. 1956. Factors affecting the bacteriostatic action of sodium nitrite. Appl. Microbial. 3: 164.

Fang, C.S., Post, L.S., and Solberg, M. 1985. Antimicrobial effect and disappearance of sodium nitrite in Staphylococcus aureas cultures. J. Food SCL 50: 1412. of n-nitroso compounds. KIV l-16. Food and Drug J. 1967. Bacteriology of repackamd pork with reference to the gas composition within the nacR. J. _ Appl. Racteriol. 30: 321. Geniaeoreis. C.. Rieman. H.. and Sadler. W.W. 1969. Production of enterot&n B-in cured mea& J. Food Sci. 34: 62. Genigeorgis, C., Savouknbs, M., and Martin, S. 1971. Initiation of.staph$~ccal growth m processed meat environments. Appl. Mmrobiol. 21: Gray,.J.L, MacDonald, D.B., Pearson, A.M., and Morton, I.D. 1981. Role of nitrite in cured meat flavor. A review. J. Food Prot. 44: 302. Heidelbauer, R.J. and Middaugh, P.R. 1973. Inhibition of staphylococcal enterotoxin production in convenience foods. J. Food Sci, 38: 885. ICMSF. 1978. Serological detection of stapbylococcal enterotoxins. In Microorganisms in Foods 1. Their Significance and Methods of Enumeration, p. 242. International Commission on Microbiological Specifications of Foods. University of Toronto Press, Toronto. In am, M. 1962. Microbiological principles in prepackaging meats. J. Appl. f?acteriol. 25: 259. Kramlich, W.E. 1978. Sausage products. Ch. 11. In The Science of Meat and Meat Products, J.F. Price and B.S. Schweigert (Ed.), p. 484. Food and Nutrition Press, Westport, CT. I.&in H.V. 1976. Equipment, media, reagents, routine tests and stains. In mpendium of Methods for the Microbiological Examination of Foods. IF &I:.: eck (Ed.), p. 27. Amencan F ublm Health Association, Washing8 MacDoug&l, D G Mottram D.S and Rhodes D.N. 1975. Contribution of nitrite and n&rates to coiour &d flavour df cured meats. J. Sci. Food Agric. 26: 1743. Notermans, S. and Heuvelman, C.J. 1983. Combined effect of water activity, pH and sub-optimal temperature on growth and exterotoxin production of Sta hylococcus aureus. J. Food Sci. 48: 1832. Pierson, M. 8 . and Smoot, L.A. 1982. Nitrite, nitrite alternatives and control of C. botulinurn in cured meats. CRC Crit. Rev. Food Sci. Nutr. 17: 141. Sebranek. J.G. and Cassens. R.G. 1973. Nitrosamines: A review. J. Milk Food Technol. 36: 76. Seideman, S.C., Vanderzent, C., Hanna, M.O., Carpenter, J.L., and Smith, G.C. 1976. Effect of various types of vacuum packages and length of storage on the microbial flora of wholesale and retail cuts of beef. J. Milk Food Technol. 39: 745. Simard. R.E.. Lee. B.H., and Laleve, C.L. 1985. Effects of temuerature and storage time on the microflora, sensory and exudate changes of vacuumor nitrogen- packed beef. Can. Inst. Food Sci. Technol. J. 18: 126. Tatini, S.R. 1973. Intluence of food environments on growth of Staphyloccoccus aureus and production of various enterotoxins. J. Milk Food Technol. 36: 659. Wasserman, A.E., Kimoto, W., and Phillips, J.G. 1977. Consumer acceptance of nitrite-free bacon. J. Food Prot. 40: 683. Ms received 2/20/811 revised 11/18/87; accepted lll18187.

New Jersey Agricultural Experiment Station Publication No. D 106X-1.87 sup parted by State Funds, by U.S. Hatch Act Funds and by Boaz,Allen and Hamilton prime contractorto the U.S. Food & Drug Administration.

DSC OF CHICKEN TISSUE PROTEINS. , .From page 370

Kijowski, J.M. and Mast, M.G. 1988. Thermal properties of proteins in chicken broiler tissues. J. Food Sci. 53: 363. Lim, J.J. 1976. Transition temperature and enthalpy change dependence on stabilizing and destabilizing ions in the helm-coil transition in native tendon collagen. Biopolymers 15: 2371. MacFarlane, J.J., McKenzie, LJ., Turner, R.H., and Jones, P.N. 1981. Pressure treatment of meat: Effects of thermal transitions and shear values. Meat Sci. 5: 307. Martens, H., Stabursvik, E., and Martens, M. 1982. Texture and colour &an s in meat during cooking related to the thermal denaturation of ~UBC K proteins. J. Tex. Stud. 13: 291. e Creshkin, E.F., Borisova, MA, Tchubarova, G.S., and Gorbatov, V.M. 1986. Conformation chanaes in the muscle oroteins of cured beef durine heating. Meat Sci. 16: 297. Pepper, F.H. and Schmidt, G.R. 1975. Effect of blending time, salt, phosphato and hot-boned beef on binding strength and cooked yield on beef rolls. J. Food Sci. 40: 227. Quinn, J.R., Raymond, D.P., and HarwaIkar, V.R. 1980. Differential scanning calorimetry of meat proteins as affected by processing treatment. J. Food Sci. 45: 1145. SAS. 1985. SAS User Guide: Statistics, Version 5 Edition. SAS Instis tute Inc., Cary, NC. Sta$rsvik, E. and Martens, H. 1980. Thermal denaturation of proteins in r mu&e tissue as studied by differential scanning calorimetry. J. Sci ood Apt. 31: 1034. T Trout, G.R. an Schmidt, G.R. 1983. Utilization of phosphates in meat products. Reciprocal Meat Conference of the American Meat Science As-

on thermal ribonuclease transition. J. Biol. Chem. 240: 3909, Wagner, J.R. and Anon, M.C. 1985. Denaturation kinetics of myofibrillar proteins in bovine muscle. J. Food Sci. 50: 1547. Wan K. 1982. Purification of titin and rebulin. In Methods in Enzymof ogy, (Ed.) S.P. Colowick and N.A. Kaplan, Vol. 86, p. 264. Academic Press, New York. Wright, D.J., Leach, LB., and Wilding, P. 1977. Differential scanning calorimetric studies of muscle and its constituent proteins. J. Sci. Food Asric. 28: 557. Wright, D.J. and Wilding, P. 1984. Differential scanning calorimetric study of muscle and its proteins: myosin and its subfragments J. Sci. Food Agric. 35: 357. Wu, MC. Akabana, T., Lamer, T.C., and Hamann, D.D. 1985. Thermal tansitions of actomyosin and surimi prepared from Atlantic croaker as studied b differential scanning calorimetry. J. Food Sci. 60: 10. MB receivei 4113187;revised 9116187;accepted 9116187.

Paper No. 7643 in the Journal Seriesof the PennsylvaniaAgricultural Experiment StatiOIl.

Volume 53, No. 2, 1988~JOURNAL

OF FOOD SCIENCE-387