Professional Documents
Culture Documents
89 (2003) 1734
Review Paper
Abstract
Cellular components of thermophilic organisms (enzymes, proteins and nucleic acids) are also thermostable. Apart from high
temperature they are also known to withstand denaturants of extremly acidic and alkaline conditions. Thermostable enzymes are highly
specific and thus have considerable potential for many industrial applications. The use of such enzymes in maximising reactions
accomplished in the food and paper industry, detergents, drugs, toxic wastes removal and drilling for oil is being studied extensively. The
enzymes can be produced from the thermophiles through either optimised fermentation of the microorganisms or cloning of fast-growing
mesophiles by recombinant DNA technology. In this review, the source microorganisms and properties of thermostable starch hydrolysing
amylases, xylanases, cellulases, chitinases, proteases, lipases and DNA polymerases are discussed. The industrial needs for such specific
thermostable enzyme and improvements required to maximize their application in the future are also suggested.
2003 Elsevier Science Ltd. All rights reserved.
Keywords: Thermostable enzymes; Thermophilic microorganisms
1. Introduction
18
0960-8524/03/$ - see front matter 2003 Elsevier Science Ltd. All rights reserved.
doi:10.1016/S0960-8524(03)00033-6
Table 1
Examples of sites serving as sources of microorganisms which can provide thermo tolerant enzymes
Source
Microorganism
Enzyme
References
Hot spring
Hot spring
Deep sea hydrothermal vent
Marine solfatare
Decomposed plant samples from
a lake
Hot spring
Compost of fermenting citrus peels,
coffee and tea extract residues
Thermus sp.
Bacillus sp. WN.11
Staphilothermus marinus
Thermococcus litoralis
Clostridium absonum CFR-702
a-Amylase
a-Amylase
a-Amylase
Pullulanase
Cellulase free xylanase
Lipase
Endochitinase
Compost
Korean salt fermented anchovy
Deep sea hydrothermal vent
Sediments of hot springs
Garbage dump
Compost treated with artichoke juice
b-N-acetylhexosaminidase
b-Amylase
Alkaline phosphatase
a-Amylase-like pullulanase
Xylanase
Inulinase
Table 2
Bioconversion reactions and applications of thermostable enzymes
Bioconversions
Applications
a-Amylase (bacterial)
90100
Starch!dextrose syrups
a-Amylase (fungal)
Pullulanase
Xylanase
Chitinase
5060
5060
4565, 105a
6575b
Starch!dextrose syrups
Starch!dextrose syrups
Craft pulp!xylan+lignin
Chitin!chitobiose
Cellulase
4555, 95c
Chitin!N-acetyl glucosamine
(chitibiase)
N-acetyl glucosamine!
glucosamine (deacetylation) Chitin!
chitosan (deacetylase)
Cellulose!glucose
Protease
6585
Lipase
3070
DNA polymerase
9095
a
Xylanase from Thermotoga sp.
b
Within this range enzyme activity was high. cCellulases
DNA amplification
4.
19
5.
Amylolytic enzymes
20
Table 3
Enzymes
Organism
Enzyme properties
Optimal temperature
C) Optimal
(
pH
References
a-Amylase
Bacillus amyloliquefaciens
Bacillus licheniformis
Bacillus stearothermophilus
Bacillus stearothermophilus
Bacillus subtilis
Lactobacillus manihotivorans
Myceliophthora thermophila
Pyrococcus furiosus
Pyrococcus woesei
Staphylothermus marinus
Sulfolobus solfataricus
Thermococcus aggreganes
Thermococcus celer
Thermococcus fumicolans
Thermococcus hydrothermalis
Thermomyces lanuginosus
Thermococcus profoundus
70
100
7080
70
70
55
100
100
100
65
100
90
95
85
60
80
7.0
6.06.5
5.06.0
7.0
5.5
5.6
5.5
6.57.5
5.0
5.5
5.5
4.06.3
4.87.8
5.6
4.05.0
Underkofler (1976)
Viara et al. (1993)
Vihinen and Mantsala (1990)
Jeayoung et al. (1989)
Canganella et al. (1994)
Aguilar et al. (2000)
Ramkrishna et al. (1993)
Laderman et al. (1993a,b)
Koch et al. (1991)
Canganella et al. (1994)
Haseltine et al. (1996)
Canganella et al. (1994)
Canganella et al. (1994)
Estelle et al. (1997)
Estelle et al. (1997)
Jensen and Olsen (1991)
Kwak et al. (1998)
b-Amylase
Bacillus circulans
60
50
50
75
60
7.5
5.5
5.86.0
Takasaki (1976a,b)
Young et al. (2001)
Shen et al. (1988)
Nipkow et al. (1989)
Bacillus sp.
60
Takasaki (1976a,b)
Pyrococcus furiosus
Pyrococcus woesi
Thermococcus aggregans
Thermus caldophilus GK24
Thermococcus celer
Thermococcus hydrothermalis
Thermococcus litoralis
Thermotoga maritima MSB8
98
100
100
75
90
95
98
90
5.5
5.56.0
6.5
5.5
5.5
5.5
5.5
6.0
Pullulanase
21
Table 4
Calcium requirement of industrially important starch degrading enzyme
6. Thermostable xylanases
Xylan, which is the dominating component of
hemicelluloses, is one of the most abundant organic
substances on earth. It has a great application in the pulp
and paper industry (Dekker and Linder, 1979; Chen et
al., 1997; Lee et al., 1998). The wood used for the
production of the pulp is treated at high temperature and
basic pH, which implies that the enzymatic procedures
require proteins exhibiting a high thermostability and
activity in a broad pH range (Jacques et al., 2000).
Treatment with xylanase at elevated temperatures
disrupts the cell wall structure. This, as a result,
facilitates lignin removal in the various stages of
bleaching. Xylanases for such a purpose (1) must lack
cellulytic activity to avoid hydrolysis of the cellulose
fibers, (2) need to be of low molecular mass to facilitate
their diffusion in the pulp fibers, and (3) most
importantly, high yields of enzyme must be obtained at a
very low cost (Niehaus et al., 1999). According to these
authors all commercially available xylanases can only
partially fulfill these requirements, and the optimum
temperature for the activity of most xylanases is reported
to be 5060 C with a half-life of about 1 h at 55 C
(Jacques et al., 2000). However, some xylanases have
been reported to exhibit higher thermal stability and
optimal activity ranging from 80 to 100 C (Saul et al.,
1995; Zverlov et al., 1996; Morris et al., 1998).
22
Microorganism
Application temperature
range (C)
Application pH
range
Bacillus subtilis
8085
6.07.0
150
Bacillus licheniformis
95105
6.07.0
20
5570
5565
5565
4.05.0
3.55.0
3.55.0
50
0
0
Fungal a-amylase
Aspergillus oryzae
Amyloglucosidase
Aspergillus niger
Pullulanase
Bacillus acidopolluliticus
Source: Hans (1995).
Table 5
Source microorganisms and properties of thermostable xylanases
Organism
Baccillus amyloliquefaciens
Bacillus circulans
Bacillus sp.
Bacillus sp. strain SPS-0
Bacillus subtilis
Clostridium abosum
Dictyoglomus sp. strain B1
Fusarium proliferatum
Pyrococcus furiosus
Pyrococcus furiosus
Scytalidium thermophilum
Streptomyces sp. strain S38
Sulfolobus solfataricus
Teheromyces lanuginosus (wild and mutant)
Teheromyces lanuginosus-SSBP
Thermoascus aurantiacus
Thermotoga maritima MSB8
Thermotoga maritima MSB8
Thermotoga maritima MSB8
Thermotoga neapolitana
Thermotoga neapolitana
Thermotoga neapolitana
Thermotoga sp. strain FjSS3-B1
Thermotoga sp. strain FjSS3-B1
Thermotoga sp. strain FjSS3-B1
Thermotoga thermarum
80
80
6075
75
50
75
90
55
100
102
65
60
105
60, 70
7075
50
92
95
75
95
85
102
80
105
115
80
Enzyme properties
Optimal temperature
C) (
6.87.0
6.07.0
8.09.0
6.0
6.0
8.5
6.07.0
5.05.5
6.0
6.0
6.0
5.3
7.0, 6.7
6.5
5.0
6.2
6.07.5
6.2
6.0
5.5
5.5
7.0
6.87.8
5.3
6.6
References
Breccia et al. (1997)
Dhillon and Khanna (2000)
Gessesse (1998)
Bataillon et al. (2000)
Paula et al. (2002)
Swaroopa and Krishna (2000)
Marjaana et al. (1994)
Badal (2002)
Bauer et al. (1999)
Kengen et al. (1993)
Nazan and Zumrut (2000)
Georis et al. (2000)
Nucci et al. (1993)
Bakalova et al. (2002)
Johnson et al. (1999)
Kalegoris et al. (1998)
Winterhalter and Liebl (1995)
Bronnenmeier et al. (1995)
Gabelsberger et al. (1993)
Bok et al. (1998)
Bok et al. (1994)
Zverlov et al. (1996)
Ruthersmith and Daniel (1991)
Ruthersmith and Daniel (1991)
Simpson et al. (1991)
Sunna et al. (1996a)
23
Table 6
Source microorganisms and properties of thermostable cellulases
8. Thermoactive chitinases
24
Organism
Enzyme properties
Optimal temperature
C) (
References
Optimal pH
Anaerocellu thermophilum
Bacillus subtilis
Pyrococcus furiosus
Pyrococcus horicoshi
Rhodothermus marinus
Thermotoga maritema MSB8
Thermotoga neapoltana
(EndocellulaseA)
Thermotoga neapoltana
(EndocellulaseB)
8590
6570
102105
97
95
95
95
5.06.6
5.06.5
6.58.0
6.07.0
6.0
106
6.06.6
cosmetics,
paper
production,
textile
finishes,
photographic products, cements, heavy metal chelating
agents and for medical and veterinary purposes (Spindler
et al., 1990; Georgopapadakou and Tkacz, 1995; Hirano,
1996; Cohen and Chet, 1998; Majeti and Kumar, 2000).
The production of chitosan from chitin involves a
deacetylation reaction that is done using 40% sodium
hydroxide solution. This is a highly corrosive stream which
is difficult to control. Attempts are thus being made to do
this conversion using deacetylase enzyme. Perhaps a
thermostable deacetylase enzyme will help in increasing
yields and conversion rates and allow reuse of the enzyme.
Endo-acting chitin hydrolase chitinaseA, the exoacting
hydrolase chitinaseB and N-acetyl-D-glucoseaminidase
are responsible for chitin degradation (Kenji et al., 1994).
However, chitin is not easily accessible to chitinases and
chitin deacetylases. Evidences from X-ray diffraction
studies have shown that chitin is a highly ordered
crystalline structure and does not dissolve in water
(Roberts, 1992). This property of chitin has shown the
need for thermostable enzymes.
The thermophilic organisms Bacillus licheniformis
X7u (Takayanagi et al., 1991), Bacillus sp. BG-11
(Bharat and Hoondal, 1998) and Strteptomyces
thermoviolaceus OPC-520 were reported to be the major
sources of chitinases (Tsujibo et al., 1995). Chitinase and
Nacetyl-glucosaminidase were produced from the
extreme
thermophilic
anaerobic
arachaeon
Thermococcus chitinophagus (Huber et al., 1995). A
thermophilic bacterium strain producing three different
endochitinases in its culture fluid was isolated from
chitin-containing compost (Kenji et al., 1994). The
strains belonged to the genus Bacillus and three isoforms
25
Table 7
Source microorganisms and properties of thermostable proteolytic enzymes
Organism
Bacillus brevis
Bacillus licheniformis
Bacillus stearothermophilus
Bacillus stearothermophilus
Bacillus sp. JB-99
Bacillus stearothermophilus TP26
Bacillus sp. no. AH-101
Bacillus thermoruber
Pyrococcus sp. KODI
Staphylothermus marinus
Thermoacidophiles
(archeal and bacterial origin)
Thermococcus aggreganes
Thermococcus celer
Thermococcus litoralis
Thermotoga maritema
Enzyme properties
Optimal temperature
C) ( Optimal pH
References
60
70
60
85
80
75
80
45
100
6070
10.5
9.0
612
12.013.0
9
7
9
7.08.5
90
95
85
95
7.0
7.5
8.5
9.5
26
Table 8
Source microorganisms and properties of thermostable lipases
Organism
Bacillus acidocaldariusa (esterase)
Bacillus sp. RSJ-1
Bacillus strin J 33a
Bacillus stearothermophilusa
Bacillus thermocatenletusa
Bacillus thermoleovorans ID-1
Geobacillus sp.
Pseudomonas sp.
Pseudomonas sp.
Pyrobaculum calidifontis
Pyrococcus furiosusa (esterase)
Pyrococcus horikoshii
Pyrococcus horikoshii
a
Enzyme properties
Optimal temperature
C) ( Optimal pH
70
50
60
68
6070
7075
70
65
90
90
100
97
95
8.09.0
8.0
8.09.0
7.5
9.0
9.6
11.0
5.6
7.0
References
Manco et al. (1998)
Sharma et al. (2002)
Nawani et al. (1998)
Gupta et al. (1999)
Klibanov (1983)
Dong-Woo et al. (1999)
Abdel-Fattah (2002)
Kulkurani and Gadre (1999)
Rathi et al. (2000)
Hotta et al. (2002)
Ikeda and Clark (1998)
Ando et al. (2002)
Yan et al. (2000)
Bacillus stearothermophilus
Pyrococcus sp. GB-D
Pyrococcus furiosus
Pyrococcus woesei
Thermus aquaticus
Thermus filiformis
Thermus flavus
Thermus thermophilus
Tma pol
Thermotoga maritema
Vent pol
Thermococcus litoralis
HF and LF, high and low fidelity; NI, not identified.
27
References
HF
LF
LF
LF
HF
NI
NI
HF
LF
LF
28
13. Conclusion
Recent investigations have demonstrated that
extremophilic archaea, bacteria and fungi have colonized
environments that were believed to be inhospitable for
survival. Their true diversity in fact, is not yet been fully
explored. The thermostable enzymes isolated from these
organisms have just started providing conversions under
conditions that are appropriate for industrial applications.
The conditions required by these thermostable enzymes
which bring about specific reactions not possible by
chemical catalysts are still mild and environmentally
benign, as compared to the temperatures and pressures
required for chemical conversions. Thus, with the
availability of thermostable enzymes a number of new
applications in the future are likely. Although, believed to
provide tremendous economical benefits, production of
the enzymes to the level required by the industries has
remained a challenge.
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