Thermozymes and their applications

Enzymes from thermophilic microorganisms, thermozymes, have unique characteristics such as temperature, chemical, and pH stability. They can be used in several industrial processes, in which they replace mesophilic enzymes or chemicals. Thermozymes are often used when the enzymatic process is compatible with existing (high-temperature) process conditions. The main advantages of performing processes at higher temperatures are reduced risk of microbial contamination, lower viscosity, improved transfer rates, and improved solubility of substrates. However, cofactors, substrates, or products might be unstable or other side reactions may occur. Recent developments show that thermophiles are a good source of novel catalysts that are of great industrial interest. Thermostable polymer-degrading enzymes such as amylases, pullulanases, xylanases, proteases, and cellulases are expected to play an important role in food, chemical, pharmaceutical, paper, pulp, and waste-treatment industries. Considerable research efforts have been made to better understand the stability of thermozymes. There are no major conformational differences with mesophilic enzymes, and a small number of extra salt bridges, hydrophobic interactions, or hydrogen bounds seem to confer the extra degree of stabilization. Currently, overexpression of thermozymes in standard Escherichia coli allows the production of much larger quantities of enzymes, which are easy to purify by heat treatment. With wider availability and lower cost, thermophilic enzymes will see more application in industry.

[1]  R. Daniel,et al.  The effect of low temperatures on enzyme activity. , 1995, The Biochemical journal.

[2]  S. Osawa,et al.  Evolutionary relationship of archaebacteria, eubacteria, and eukaryotes inferred from phylogenetic trees of duplicated genes. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[3]  D. Cowan,et al.  The specific activities of mesophilic and thermophilic proteinases. , 1987, The International journal of biochemistry.

[4]  K. Myambo,et al.  DNA sequencing with Thermus aquaticus DNA polymerase and direct sequencing of polymerase chain reaction-amplified DNA. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[5]  G. Antranikian,et al.  Purification and Properties of a Thermostable Pullulanase from a Newly Isolated Thermophilic Anaerobic Bacterium, Fervidobacterium pennavorans Ven5 , 1997, Applied and environmental microbiology.

[6]  Stephen H. Brown,et al.  Characterization of Amylolytic Enzymes, Having Both α-1,4 and α-1,6 Hydrolytic Activity, from the Thermophilic Archaea Pyrococcus furiosus and Thermococcus litoralis , 1993 .

[7]  G. Barbier,et al.  New thermostable enzymes for crop fractionation , 1997 .

[8]  R. Daniel,et al.  Immobilization of a proteinase from the extremely thermophilic organism Thermus Rt41A , 1994, Biotechnology and bioengineering.

[9]  John C. Roberts,et al.  Biobleaching effect of Streptomyces thermoviolaceus xylanase preparations on birchwood kraft pulp , 1996 .

[10]  R. Rella,et al.  Thermostable β-galactosidase from the archaebacterium Sulfolobus solfataricus Purification and properties , 1990 .

[11]  R. Jaenicke,et al.  Stability and folding of ultrastable proteins: eye lens crystalline and enzymes from thermophiles 1 , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[12]  C. Biliaderis,et al.  Amylolytic enzymes and products derived from starch: a review. , 1995, Critical reviews in food science and nutrition.

[13]  M. Rossi,et al.  Industrial‐scale production and rapid purification of an archaeal beta‐glycosidase expressed in Saccharomyces cerevisiae , 1995, Biotechnology and applied biochemistry.

[14]  J. Chaudhuri,et al.  Biocatalysis in organic media using enzymes from extremophiles , 1999 .

[15]  A. Klibanov,et al.  The mechanisms of irreversible enzyme inactivation at 100C. , 1985, Science.

[16]  T. Kudo,et al.  Cloning, nucleotide sequence, and hyperexpression of α-amylase gene from an archaeon, Thermococcus profundus , 1996 .

[17]  D. Cowan,et al.  A correlation between protein thermostability and resistance to proteolysis. , 1982, The Biochemical journal.

[18]  J. Kellermann,et al.  Purification and properties of an amylopullulanase, a glucoamylase, and an alpha-glucosidase in the amylolytic enzyme system of Thermoanaerobacterium thermosaccharolyticum. , 1998, Bioscience, biotechnology, and biochemistry.

[19]  P. Nigam,et al.  Enzyme and microbial systems involved in starch processing. , 1995 .

[20]  M. Adams,et al.  Release of lignin from kraft pulp by a hyperthermophilic xylanase from Thermatoga maritima , 1997 .

[21]  T. Sekiguchi,et al.  Protein Thermostability: Mechanism and Control Through Protein Engineering , 1988 .

[22]  A. Stams,et al.  Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. , 1993, European journal of biochemistry.

[23]  Ragone,et al.  Helix-stabilizing factors and stabilization of thermophilic proteins: an X-ray based study. , 1998, Protein engineering.

[24]  D. Montgomery,et al.  Higher Ploidy in Saccharomyces cerevisiae Supports Enhanced Hepatitis B Virus S Cloned Gene Expression at the Pilot Scale , 1996, Biotechnology progress.

[25]  J. Oost,et al.  Synthesis of oligosaccharides catalyzed by thermostable β-glucosidase fromPyrococcus furiosus , 1998 .

[26]  D. Haltrich,et al.  Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable beta-glycosidases. , 1999, Biotechnology and bioengineering.

[27]  M. Rao,et al.  Application of Xylanase from Alkaliphilic Thermophilic Bacillus sp. NCIM 59 in biobleaching of bagasse pulp , 1996 .

[28]  C. Vieille,et al.  Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus , 1997 .

[29]  T. Sekiguchi,et al.  Protein engineering for thermostability. , 1990, Trends in biotechnology.

[30]  G. Antranikian,et al.  Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli , 1995, Applied and environmental microbiology.

[31]  Co-operativity of hexamer ligation. , 1996, Gene.

[32]  L. Dijkhuizen,et al.  Federal Republic of Germany , 1985, International Journal of Comparative Labour Law and Industrial Relations.

[33]  Hyun-Soo Lee,et al.  Production of cyclodextrin using raw corn starch without a pretreatment , 1997 .

[34]  R. Starnes.  Industrial potential of cyclodextrin glycosyl transferases , 1990 .

[35]  C. Vieille,et al.  Thermozymes: Identifying molecular determinants of protein structural and functional stability , 1996 .

[36]  D. Clark,et al.  Pressure-enhanced activity and stability of a hyperthermophilic protease from a deep-sea methanogen , 1997, Applied and environmental microbiology.

[37]  M. Rao,et al.  Molecular and biotechnological aspects of xylanases. , 1999, FEMS microbiology reviews.

[38]  M. Ikehara,et al.  Phosphorylating agent for the synthesis of oligonucleotide with aliphatic amino group at 5′ end , 1987 .

[39]  L. Fischer,et al.  Catalytical Potency of β-Glucosidase from the Extremophile Pyrococcus furiosus in Glucoconjugate Synthesis , 1996, Bio/Technology.

[40]  W. Zimmermann,et al.  β-Galactooligosaccharide synthesis with β-galactosidases from Sulfolobus solfataricus, Aspergillus oryzae, and Escherichia coli ☆ , 1999 .

[41]  N Jenkins,et al.  Glycosylation of recombinant proteins: problems and prospects. , 1994, Enzyme and microbial technology.

[42]  F. Barany.  Genetic disease detection and DNA amplification using cloned thermostable ligase. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[43]  J. Janin,et al.  Arginine residues as stabilizing elements in proteins. , 1993, Biochemistry.

[44]  G. Antranikian,et al.  Extremophiles as a source of novel enzymes for industrial application , 1999, Applied Microbiology and Biotechnology.

[45]  Š. Janeček,et al.  Thermophilic archaeal amylolytic enzymes , 2000 .

[46]  T. D. Brock.  Life at High Temperatures , 1985, Science.

[47]  T. Kudo,et al.  Purification and characterization of α-amylase from hyperthermophilic archaeon Thermococcus profundus, which hydrolyzes both α-1,4 and α-1,6 glucosidic linkages , 1998 .

[48]  R. Daniel,et al.  The use of proteases from extreme thermophiles for meat tenderisation. , 1992, Meat science.

[49]  W. Quax.  THERMOSTABLE GLUCOSE ISOMERASES , 1993 .

[50]  L. Wyns,et al.  The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures , 1999, Proteins.

[51]  Michael L. Kotewicz,et al.  Isolation of cloned Moloney murine leukemia virus reverse transcriptase lacking ribonuclease H activity , 1988, Nucleic Acids Res..

[52]  J. Wiegel,et al.  Purification and cloning of a thermostable xylose (glucose) isomerase with an acidic pH optimum from Thermoanaerobacterium strain JW/SL-YS 489 , 1996, Journal of bacteriology.

[53]  W. Liebl,et al.  Properties and gene structure of the Thermotoga maritima alpha-amylase AmyA, a putative lipoprotein of a hyperthermophilic bacterium , 1997, Journal of bacteriology.

[54]  B. Matthews,et al.  Structural and genetic analysis of protein stability. , 1993, Annual review of biochemistry.

[55]  John C. Roberts,et al.  Bleach Boosting Effect of Cellulase-free Xylanase of Streptomyces Thermoviolaceus and its Comparison with Two Commercial Enzyme Preparations on Birchwood Kraft Pulp , 1998 .

[56]  What ultrastable globular proteins teach us about protein stabilization. , 1998, Biochemistry. Biokhimiia.

[57]  R. Jaenicke,et al.  Protein stability and molecular adaptation to extreme conditions. , 1991, European journal of biochemistry.

[58]  R. Kelly,et al.  Proteases and glycosyl hydrolases from hyperthermophilic microorganisms. , 1996, Advances in protein chemistry.

[59]  R. Daniel,et al.  The upper limits of enzyme thermal stability , 1996 .

[60]  G. Antranikian,et al.  Pullulanase Type I from Fervidobacterium pennavorans Ven5: Cloning, Sequencing, and Expression of the Gene and Biochemical Characterization of the Recombinant Enzyme , 1999, Applied and Environmental Microbiology.

[61]  O. Kandler,et al.  Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[62]  S. d'Auria,et al.  Structure-function studies on beta-glycosidase from Sulfolobus solfataricus. Molecular bases of thermostability. , 1998, Biochimie.

[63]  J. Zeikus.  Molecular determinants of thermozyme activity and stability: Analysis of xylose isomerase and amylo-pullulanase , 1996 .

[64]  J. Trela,et al.  Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus , 1976, Journal of bacteriology.

[65]  M. Kearsley,et al.  Handbook of Starch Hydrolysis Products and their Derivatives , 1995 .

[66]  L. Dijkhuizen,et al.  Characterization of a new Bacillus stearothermophilus isolate: a highly thermostable α-amylase-producing strain , 1994, Applied Microbiology and Biotechnology.

[67]  Y. Nonaka,et al.  The thermolysin-catalyzed condensation reactions of n-substituted aspartic and glutamic acids with phenylalanine alkyl esters , 1979 .

[68]  F. Duchiron,et al.  Purification and properties of a thermoactive and thermostable pullulanase from Thermococcushydrothermalis, a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent , 1998, Applied Microbiology and Biotechnology.

[69]  R. Daniel,et al.  Laboratory-scale investigations into the use of extremely thermophilic proteinases for cleaning ultrafiltration membranes fouled during whey processing , 1992 .