Abstract
Microorganisms living in extreme environmental conditions (extremophiles) are potential source of extremozymes; they possess utmost stability under extreme environmental conditions. Cold-active enzymes are extremozymes produced by the psychrophiles (extremophiles) and have attracted much attention as biocatalysts due to their capacity to resist unfavourable reaction conditions in the industrial process. Cold-active enzymes possess wide applications in the food industry; these enzymes are not only secreted by bacteria but also from yeasts and moulds. Although enzymes are derived from plant and animal sources, cold-active microbial enzymes have taken advantage, due to their productivity and thermostability. Psychrophilic microorganisms produce a wide range of cold-active enzymes with immune application in food processing. The use of ß-galactosidase for the removal of lactose from refrigerated milk, application of pectinase for the reduction of viscosity and turbidity in chilled juice and use of amylase for hydrolysis of polysaccharides in starch processing industries and processing of meat with the help of cold-active proteases are the representative examples of application of cold-active enzymes. Cold-active enzymes possess exceptional molecular flexibility that has opened up newer areas of applications. In food processing industries, cold-active pectinases have been used for the removal of pectin which is important in fruit juice and wine processing, coffee and tea processing and macerating of plants and vegetable tissue, for degumming of plant fibres, for extracting vegetable oils and for adding poultry feed and in the alcoholic beverages. To fulfil the demand of industries, enzyme technology needs extension of biotechnological approach in terms of both quality and quantity. The potential of cold-active enzymes provides numerous opportunities for industrial applications. However, specific properties of cold-active enzymes may be improved and modified through enzyme engineering.
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References
Abdou AM (2003) Purification and partial characterization of psychrotrophic Serratia marcescens lipase. J Dairy Sci 86:127–132
Adams MWW, Perler FB, Kelly RM (1995) Extremozymes: expanding the limits of biocatalysis. Biotechnology 13:662–668
Adapa V, Ramya LN, Pulicherla KK, Rao KR (2014) Cold active pectinases: advancing the food industry to the next generation. Appl Biochem Biotechnol 172:2324–2337
Aghajari N, Feller G, Gerday C, Haser R (1998) Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level. Structure 6:1503–1516
Alkorta I, Garbisu C, Llama MJ, Serra JL (1998) Industrial applications of pectic enzymes: a review. Process Biochem (London) 33:21–28
Alquati C, De Gioia L, Santarossa G, Alberghina L, Fantucci P, Lotti M (2002) The cold-active lipase of Pseudomonas fragi: heterologous expression, biochemical characterization and molecular modeling. Eur J Biochem 269:3321–3328
Aoyama S, Yoshida N, Inouye S (1988) Cloning, sequencing and expression of the lipase gene from Pseudomonas fragi IFO-12049 in E. coli. FEBS Lett 242:36–40
Aurilia V, Parracino A, D’Auria S (2008) Microbial carbohydrate esterases in cold adapted environments. Gene 410:234–240
Bakermans C, Skidmore ML (2011) Microbial metabolism in ice and brine at −5 degrees C. Environ Microbiol 13:2269–2278
Baracat MC, Vanetti MCD, Araujo EF, Silva DO (1991) Growth conditions of a pectinolytic Aspergillus fumigatus for degumming of natural fibres. Biotechnol Lett 13:693–696
Białkowska A, Cieslin’ski H, Nowakowska K, Kur J, Turkiewicz M (2009) A new β-galactosidase with a low temperature optimum isolated from the Antarctic Arthrobacter sp. 20B: gene cloning, purification and characterization. Arch Microbiol 191:825–835
Bonnin E (2003) Mode of action of Fusarium moniliforme endopolygalacturonase towards acetylated pectin. Carbohydr Polym, Amsterdam 52:381–388
Borchert TV, Svendsen A, Andersen C, Nielsen B, Nissem TL, Kjaerulff S (2004) Exhibit alterations in at least one of the following properties relative to parent alpha-amylase: improved pH stability at pH 8–10.5, improved calcium ion stability at pH 8–10.5, increased specific activity at 10–60°C. US Patent No 6673589 B2
Braga AA, De Morais PB, Linrdi VR (1998) Screening of yeasts from Brazilian Amazon rain forest for extracellular proteinases production. Syst Appl Microbiol 21:353–359
Buisman GJH, Helteren CTW, Kramer GFH, Veldsink JW, Derksen JTP, Cuperus FP (1998) Enzymatic esterifications of functionalized phenols for the synthesis of lipophilic antioxidants. Biotechnol Lett 20:131–136
Burhan A, Nisa U, Gokhan C, Omer C, Ashabil A, Osman G (2003) Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6. Process Biochem 38:1397–1403
Bury D, Jelen P, Kalab M (2001) Disruption of Lactobacillus delbrueckii sp. Bulgaricus 11842 cells of lactose hydrolysis in dairy products: a comparison of sonication, high pressure homogenization and bead milling. Innovative Food Sci Emerg Technol 2(1):23–29
Carrara CR, Rubiolo AC (1994) Immobilization of β-galactosidase on chitosan. Biotechnol Prog 10(2):220–224
Cavicchioli R, Siddiqui KS (2004) Cold adapted enzymes. In: Pandey A, Webb C, Soccol CR, Larroche C (eds) Enzyme technology. Asiatech Publishers, New Delhi, pp 615–638
Cavicchioli R, Thomas T (2000) Extremophiles. In: Lederberg J, Alexander M, Bloom BR et al (eds) Encylopedia of microbiology, 2nd edn. Academic, San Diego, pp 317–337
Cavicchioli R, Siddiqui KS, Andrews D, Sowers KR (2002) Low temperature extremophiles and their applications. Curr Opin Biotechnol 13:253–261
Chen S, Kaufman MG, Miazgowicz KL et al (2013) Molecular characterization of a cold-active recombinant xylanase from Flavobacterium johnsoniae and its applicability in xylan hydrolysis. Bioresour Technol 128:145–155
Coker J, Peter P, Loveland J, Brenchley JE (2003) Biochemical characterization of a β-galactosidase with a low temperature optimum obtained from an Antarctic Arthrobacter isolate. J Bacteriol 185:5473–5482
Collins T, Meuwis MA, Stals I et al (2002) A novel family 8 xylanase, functional and physicochemical characterization. J Biol Chem 277:35133–35139
Collins T, Gerday C, Feller G (2005) Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol Rev 29:3–23
Collmer A, Ried JL, Mount MS (1988) Assay methods for pectic enzymes. Meth Enzymol 161:329–335
Cowan DA, Casanueva A, Stafford W (2007) Ecology and biodiversity of cold-adapted microorganisms. In: Physiology and biochemistry of extremophiles. American Society of Microbiology, Washington, DC
D’Amico S, Marx J-C et al (2003) Activity-stability relationships in extremophilic enzymes. J Biol Chem 278(10):7891–7896
D’Amico S, Collins T, Marx JC et al (2006) Psychrophilic microorganisms: challenges for life. EMBO Rep 7:385–389
Dahiya N, Tewari R, Hoondal GS (2006) Biotechnological aspects of chitinolytic enzymes: a review. Appl Microbiol Biotechnol 71:773–782
De Maayer P, Anderson D, Cary C, Cowan DA (2014) Some like it cold: understanding the survival strategies of psychrophiles. EMBO Rep 15:508–517
Del-Cid A, Ubilla P, Ravanal MC et al (2014) Cold-active xylanase produced by fungi associated with Antarctic marine sponges. Appl Biochem Biotechnol 172:524–532
Deming JW (2002) Psychrophiles and polar regions. Curr Opin Microbiol 5:301–309
Dewan SS (2014) Global markets for enzymes in industrial applications. BCC Research, Wellesley
Dieckelmann M, Johnson LA, Beacham IR (1998) The diversity of lipases from psychrotrophic strains of Pseudomonas: a novel lipase from a highly lipolytic strain of Pseudomonas fluorescens. J Appl Microbiol 85:527–536
Dornez E, Verjans P, Arnaut F, Delcour JA, Courtin CM (2011) Use of psychrophilic xylanases provides insight into the xylanase functionality in bread making. J Agric Food Chem 59:9553–9562
Fadel M (2000) Production of thermostable amyletic enzymes by A. niger F-909 under SSF. Egypt J Microbiol 35:487–505
Farrell J, Rose AH (1967) Temperature effects on microorganisms. In: Rose AH (ed) Thermobiology. Academic, London, pp 147–218
Feller G (2013) Psychrophilic enzymes: from folding to function and biotechnology. Scientifica (Cairo) 2013:512840
Feller G, Gerday C (2003) Psychrophilic enzymes: hot topics in cold adaptation. Nat Rev Microbiol 1:200–208
Feller G, Narinx E, Arpigny JL et al (1996) Enzymes from psychrophilic organisms. FEMS Microbiol Rev 18:189–202
Feller G, Le Bussy O, Gerday C (1998) Expression of psychrophilic genes in mesophilic hosts: assessment of the folding state of a recombinant α-amylase. Appl Environ Microbiol 64:1163–1165
Fernandez S, Geueke B, Delgado O (2002) β-galactosidase from a cold-adapted bacterium: purification, characterization and application for lactose hydrolysis. Appl Microbiol Biotechnol 58:313–321
Georlette D, Blaise V, Collins T et al (2004) Some like it cold: biocatalysis at low temperatures. FEMS Microbiol Rev 28:25–42
Gerday C, Aittaleb M, Bentahir M et al (2000) Cold-adapted enzymes: from fundamentals to biotechnology. Trends Biotechnol 18:103–107
Ghosh M, Pulicherla KK, Rekha VP et al (2012) Cold active beta-galactosidase from Thalassospira sp. 3SC-21 to use in milk lactose hydrolysis: a novel source from deep waters of Bay-of-Bengal. World J Microbiol Biotechnol 28:2859–2869
Goodchild A, Saunders NFW, Ertan H et al (2004) A proteomic determination of cold adaptation in the Antarctic archaeon, Methanococcoides burtonii. Mol Microbiol 53:309–321
Gounot AM (1991) Bacterial Life at low temperature: physiological aspects and biotechnological implications. J Appl Bacteriol 71:386–397
Gummadi SN, Panda T (2003) Purification and biochemical properties of microbial pectinases: a review. Process Biochem, Barking 38:987–996
Haki GD, Rakshit SK (2003) Developments in industrially important thermostable enzymes: a review. Bioresour Technol 89:17–34
Hamid B (2016) Cold-active α-amylase from psychrophilic and psychrotolerant yeasts. J Global Biosci 7:2670–2677
Hamid B, Singh P, Mohiddin FA et al (2013) Partial characterization of cold-active β-galactosidase activity produced by Cystophallobaidium capatitum SPY11 and Rodotorell amusloganosa PT1. J Endocytobiosis Cell Res 24:23–26
Hamid B, Ravinder SR, Deepak C et al (2014) Psychrophilic yeasts and their biotechnological applications – a review. Afr J Biotechnol 13(22):2188–2197
Haseltine C, Rolfsmeier M, Blum P (1996) The glucose effect and regulation of amylase synthesis in the hyperthermophilic archaeon Sulfolobus solfataricus. J Bacteriol 178:945–950
Hatti-Kaul R, Birgisson HO, Mattiasson B (2006) Cold active enzymes in food processing. In: Shetty K, Paliyath G, Pometto A, Levin RE (eds) Food Biotechnology, 2nd edn. CRC, Taylor & Francis, Boca Raton, pp 1631–1653
Helmke E, Weyland H (2004) Psychrophilic versus psychrotolerant bacteria-occurrence and significance in polar and temperate marine habitats. Cell Mol Biol 50:553–561
Horikoshi K (1999) Alkaliphiles: some applications of their products for biotechnology. Microbiol Mol Biol Rev 63:735–750
Hough DW, Danson MJ (1999). Extremozymes) Curr Opin Chem Biol 3:39–46
Hoyoux A, Jennes I, Gerday C (2001) Cold-adapted β-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis. Appl Environ Microbiol 67:1529–1535
Jaeger and Eggert (2002) Lipases for biotechnology. Curr Opin Biotechnol 13(4):390–397
Horner TW, Dunn ML, Eggett DL, Ogden LV (2011) Beta-galactosidase activity of commercial lactase samples in raw and pasteurized milk at refrigerated temperatures. J Dairy Sci 94:3242–3249
Joseph B (2006) Isolation, purification and characterization of cold adapted extracellular lipases from psychrotrophic bacteria: feasibility as laundry detergent additive. Ph.D thesis, Allahabad Agricultural Institute Deemed University, India
Kuddus M, Ramteke PW (2008) Purification and properties of cold-active metallo protease from Curtobacterium luteum and effect of culture conditions on production. Chin J Biotechnol 24:2074–2080
Kuddus M, Saima R, Ahmad IZ (2012) Cold-active extracellular α-amylase production from novel bacteria microbacterium foliorum GA2 and Bacillus cereus GA6 isolated from Gangotri glacier, Western Himalaya. J Genet Eng Biotechnol 10:151–159
Kunamneni A, Plou FJ, Ballesteros A et al (2008) Laccases and their applications: a patent review. Recent Pat Biotechnol 2:10–24
Lambo A, Patel T (2006) Cometabolic degradation of polychlorinated biphenyls at low temperature by psychrotolerant bacterium Hydrogenophaga sp. IA3-A. Curr Microbiol 53(1):48–52
MacElroy RD (1974) Some comments on the evolution of extremophiles. Biosystems 6:74–75
Madigan MT, Marrs BL (1997) Extremophiles. Sci Am 276:66–71
Margesin R, Schinner F (1994) Properties of cold-adapted microorganisms and their potential role in biotechnology. J Biotechnol 33:1–14
Margesin R, Feller G, Gerday C et al (2002) Cold-adapted microorganisms: adaptation strategies and biotechnological potential. In: Bitton G (ed) The encyclopedia of environmental microbiology, vol 2. Wiley, New York, pp 871–885
Mateo C, Monti R, Pessela BC et al (2004) Immobilization of lactase from Kluyveromyces lactis greatly reduces the inhibition promoted by glucose. Full hydrolysis of lactose in milk. Biotechnol Prog 20:1259–1262
Morita RY (1966) Marine psychrophilic bacteria oceanoger. Mar Biol Ann Rev 4:105–121
Morita RY (1975) Psychrophilic bacteria. Bacteriol Rev 39:144–167
Mykytczuk NC, Foote SJ, Omelon CR et al (2013) Bacterial growth at -15°C; molecular insights from the permafrost bacterium Planococcus halocryophilus Or1. ISME J 7:1211–1226
Nakagawa T, Yamada K, Miyaji T, Tomizuka N (2002) Cold-active pectinolytic activity of psychrophilic-basidiomycetous yeast Cystofilobasidium capitatum strain PPY-1. J Biosci Bioeng 94:175–177
Nakagawa T, Fujimoto Y, Uchino M et al (2003) Isolation and characterization of psychrophiles producing cold-active β-galactosidase. Lett Appl Microbiol 37:154–157
Nakagawa T, Nagaoka T, Taniguchi S et al (2004) Isolation and characterization of psychrophilic yeasts producing cold-adapted pectinolytic enzymes. Lett Appl Microbiol 38:383–387
Nakagawa T, Ikehata R, Uchino M (2006a) Cold-active β-galactosidase activity of isolated psychrophilic basidiomycetous yeast Guehomyces pullulans. Microbiol Res 161:75–79
Nakagawa T, Fujimoto Y, Ikehata R (2006b) Purification and molecular characterization of cold-active β-galactosidase from Arthrobacter psychrolactophilus strain F2. Appl Microbiol Biotechnol 72:720–725
Neklyudov AD, Ivankin AN, Berdutina AV (2000) Properties and uses of protein hydrolysates (review). Appl Biochem Microbiol 36:452–459
Pandey A, Nigam P, Soccol CR et al (2000) Advances in microbial amylases. Biotechnol Appl Biochem 31:135–152
Park JW, Oh YS, Lim JY et al (2006) Isolation and characterization of cold-adapted strains producing β-galactosidase. J Microbiol 44:396–402
Pilnik W, Rombouts FM (1985) Polysaccharides and food processing. Carbohydr Res 142:93–105
Pivarnik LF, Senecal AG, Rand AG (1995) Hydrolytic and transgalactosylic activities of commercial beta-galactosidase (lactase) in food processing. Adv Food Nut Res 38:1–102
Pulicherla KK, Mrinmoy G, Kumar S et al (2011) Psychrozymes – the next generation industrial enzymes. J Mar Sci Res Dev 1:102
Pulicherla KK, Kumar PS, Manideep K, Rekha VP, Ghosh M, Sambasiva Rao KR (2013) Statistical approach for the enhanced production of cold-active beta-galactosidase from Thalassospira frigidphilosprofundus: a novel marine psychrophile from deep waters of bay of Bengal. Prep Biochem Biotechnol 43:766–780
Qin Y, Huang Z, Liu Z (2014) A novel cold-active and salt-tolerant alpha-amylase from marine bacterium Zunongwangia profunda: molecular cloning, heterologous expression and biochemical characterization. Extremophiles 18:271–281
Reid I, Ricard M (2002) Pectinase in papermaking: solving retention problems in mechanical pulp bleached with hydrogen peroxide. Enzym Microb Technol 26:115–123
Rothschild LJ, Manicinelli RL (2001) Life in extreme environments. Nature 409:1092–1101
Ruberto L, Vazquez S, Lobalbo A et al (2005) Psychrotolerant hydrocarbon-degrading Rhodococcus strains isolated from polluted Antarctic soils. Antarct Sci 17(1):47–56
Russell NJ (2000) Towards a molecular understanding of cold activity of enzymes from psychrophiles. Extreamophiles 4:83–90
Russell NJ, Hamamoto T (1998) In: Horikoshi K, Grant WD (eds) Psychrophiles in extremophiles: microbial life in extreme environments. Wiley-Liss, New York, pp 25–45
Sabri A, Bare G, Jacques P (2001) Influence of moderate temperatures on myristoyl-CoA metabolism and acyl-CoA thioesterase activity in the psychrophilic antarctic yeast Rhodotorula aurantiaca. J Biol Chem 276(16):12691–12696
Sahay S, Hamid B, Singh P et al (2013) Evaluation of pectinolytic activities for oenological uses from psychrotrophic yeasts. Lett Appl Microbiol 5(2):115–121
Sakai T, Sakamoto T, Hallaert J et al (1993) Pectin, pectinase and protopectinase: production, properties, and applications. Adv Appl Microbiol 39:213–294
Schmidt NS (1902) Uebereinig epsychrophile Mikroorganismen und ihrVorkommen. Centr Bakteriol Parasitenk, Abt II 9:145–147
Shukla TP, Wierzbicki LE (1975) β-galactosidase technology: a solution to the lactose problem. Food Sci Nutr 25:325–356
Soares MMCN (2001) Pectinolytic enzyme production by Bacillus sp. and their potential application on juice extraction. World J Microbiol Biotechnol, Dordrecht 17:79–82
Speer E (1998) Milk and dairy product technology. Marcel Dekker, New York
Stokes JL (1963) General biology and nomenclature of psychrophilic microorganisms. Recent progress in microbiology VIII. University of Toronto Press, Toronto, pp 187–192
Suarez FL, Savaiano DA, Levitt MD (1995) Review article: the treatment of lactose intolerance. Aliment Pharmacol Ther 9(6):589–597
Tan S, Owusu ARK, Knapp J (1996) Low temperature organic phase biocatalysis using cold-adapted lipase from psychrotrophic Pseudomonas P38. Food Chem 57:415–418
Trindade RC, Resende MA, Silva CM et al (2002) Yeasts associated with fresh and frozen pulps of Brazilian tropical fruits. Syst Appl Microbiol 25:294–300
Truong LV, Tuyen H, Helmke E et al (2001) Cloning of two pectate lyase genes from the marine Antarctic bacterium Pseudoalteromonas haloplanktis strain ANT/505 and characterization of the enzymes. Extremophiles 5:35–44
Tutino ML, di Prisco G, Marino G et al (2009) Cold-adapted esterases and lipases: from fundamentals to application. Protein Pept Lett 16:1172–1180
Tweedie LS, MacBean RD, Nickerson TA (1978) Present and potential uses for lactose and some lactose derivative. Food Technol Assoc Australia 30:57–62
Ueda M, Goto T, Nakazawa M, Miyatake K et al (2010) A novel cold-adapted cellulase complex from Eisenia fetida: characterization of a multienzyme complex with carboxymethylcellulase, β-glucosidase, β-1,3glucanase, and β-xylosidase. Comp Biochem Physiol B Biochem Mol Biol 157:26–32
Van den Burg B (2003) Extremophiles as a source for novel enzyme. Corr Opin Microbiol 6:213–218
Wang F, Hao J, Yang C, Sun M (2010) Cloning, expression, and identification of a novel extracellular cold-adapted alkaline protease gene of the marine bacterium strain YS-80-122. Appl Biochem Biotechnol 162:1497–1505
Ward OP (1985) Proteolytic enzymes. In: Moo-Young M (ed) Comprehensive biotechnology, the practice of biotechnology: current commodity products, vol 3. Pergamon Press, Oxford, pp 789–818
Welander U (2005) Microbial degradation of organic pollutants in soil in a cold climate. Soil Sediment Contam 14(3):281–291
Wang SY, Hu W, Lin XY, Wu ZH, Li YZ (2012) A novel cold-active xylanase from the cellulolytic myxobacterium Sorangium cellulosum So9733-1: gene cloning, expression, and enzymatic characterization. Appl Microbiol Biotechnol 93:1503–1512
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Hamid, B., Mohiddin, F.A. (2018). Cold-Active Enzymes in Food Processing. In: Kuddus, M. (eds) Enzymes in Food Technology. Springer, Singapore. https://doi.org/10.1007/978-981-13-1933-4_19
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