Cold active lipases – an update

Figures & data

Figure 1. Catalytic Canonical α/β hydrolase fold of lipases.

Table 1. Microorganisms producing cold active lipase.

Microorganism	Sources	References
Bacteria
Acinetobacter sp. 6	Siberian tundra soil	Suzuki et al. (2001)
Acinetobacter baumannii BD5	Mountain water	Park et al. (2009)
Aeromonas sp. LPB4	Sea sediments	Lee et al. (2003)
Aeromonas hydrophila	Food products	Imbert and Gancel (2004)
Bacillus psychrosaccharolyticus	Soil and lowland marshes	Seo et al. (2004)
Bacillus sphaericus MTCC7526	Gangotri glacier (western Himalayas)	Joseph and Ramteke (2013)
Colwellia psychrerythraea 34H	Arctic marine sea	Do et al. (2013)
Desulfotalea psychrophila	Arctic sediments	Rabus et al. (2004)
Halomonas sp. BRI 8	Antarctic habitat	Jadhav et al. (2013)
Janibacter sp. HTCC2649	Marine habitat	Yuan et al. (2014)
Micrococcus roseus	Glacial soil	Joseph et al. (2011)
Microbacterium phyllosphaerae MTCC 7530 and Corynebacterium paurametabolum MTCC 6841	Naukuchiatal lake (western Himalayas)	Joshi et al. (2006)
Microbacterium luteolum	Gangotri glacier (western Himalayas)	Joseph et al. (2012)
Moritella sp. 2-5-10-1	Antarctic bacteria	Wang et al. (2013)
Pelagibacterium halotolerans B2T	East China Sea	Wei et al. (2013)
Photobacterium sp. MA1-3	Blood clam	Kim et al. (2012)
Photobacterium aplysiae sp. (GMD509)	Eggs of sea hare	Seo et al. (2005)
Photobacterium lipolyticum M37	Marine habitat	Ryu et al. (2006)
Photobacterium ganghwense sp. FR1311T	Deep sea	Park et al. (2006)
Photobacterium marinum AK15(T) and AK18	Sea sediment	Srinivas et al. (2013)
Pseudoalteromonas sp. wp27	Deep-sea sediments	Zeng et al. (2004)
Pseudoalteromonas sp.	Antarctic marine	Lo Giudice et al. (2006)
Pseudoalteromonas haloplanktis TAC125	Antarctic seawater	de Pascale et al. (2008)
Pseudomonas antarctica sp.	Antarctica	Reddy et al. (2004)
Pseudomonas fluorescens	Refrigerated human placental extracts	Preuss et al. (2001)
Pseudomonas fluorescens	Soil of cold region	Leonov (2010)
Pseudomonas fragi IFO3458	Ns	Alquati et al. (2002)
Pseudomonas putida GR12-2	Arctic plant	Muryoi et al. (2004)
Pseudomonas sp. MSI057	Marine sponge Dendrilla nigra	Kiran et al. (2008)
Pseudomonas sp. 42A2	Oil-contaminated water sample	Bofill et al. (2010)
Pseudomonas sp. VITCLP4	Tropical seacoast	Kavitha and Shanthi (2013)
Pseudomonas sp. AMS8	Antarctic soil	Ali et al. (2013)
Psychrobacter sp., Vibrio sp. and Pseudomonas sp. KB700A	Subterranean environment	Rashid et al. (2001)
Psychrobacter cryohalolentis K5T	Siberian cryopeg	Novototskaya-Vlasova et al. (2013)
Psychrobacter okhotskensis	Sea coast	Yumoto et al. (2003)
Psychrobacter sp. Ant300	Antarctic habitat	Kulakovaa et al. (2004)
Psychrobacter sp. wp37	Deep-sea sediments	Zeng et al. (2004)
Psychrobacter sp. 7195	Antarctic habitat	Jinwei et al. (2007)
Psychrobacter sp.	Antarctic habitat	Parra et al. (2008)
Psychrobacter sp. G	Antarctic seawater	Xuezheng et al. (2010)
Psychrobacter sp. TA144	Antarctic seawater	De Santi et al. (2010)
Psychrobacter sp. C18	Deep-sea sediments	Chen et al. (2010)
Serratia marcescens	Raw milk	Abdou (2003)
Shewanella sp. SIB1	Water deposits in oil reservoir	Suzuki et al. (2004)
Staphylococcus epidermidis	Frozen fish samples	Joseph et al. (2006)
Stenotrophomonas maltophilia CGMCC 4254	Oil soil	Li et al. (2013)
Vibrio ruber sp. Nov VR1T	Seawater	Shieh et al. (2003)
Fungi/Yeast
Aspergillus nidulans	Ns	Mayordomo et al. (2000)
Candida antarctica	Antarctic habitat	Patkar et al. (1993); Uppenberg et al. (1994b); Uppenberg et al. (1994a); Zhang et al. (2003); Siddiqui and Cavicchioli (2005)
C. albicans ATCC 10231	Ns	Lan et al. (2011)
Geomyces sp. P7	Antarctic habitat	Florczaka et al. (2013)
Geotrichum sp. SYBC WU-3	Subtropical	Cai et al. (2009)
Pichia lynferdii NRRL Y-7723	Ns	Kim et al. (2010)

Note: NS, not specified.

Table 2. Industrial applications of cold active lipases.

Application	Purpose	Source of lipase	References
Detergent industry	Detergent additive	CAL-B from Candida antarctica	Uppenberg et al. (1994a)
		Microbacterium phyllosphaerae and Bacillus sphaericus	Joseph and Ramteke (2013)
Medical and pharmaceutical applications	Synthesis of optically active amines	Candida antarctica and Pseudomonas sp	Smidt et al. (1996)
	Synthesis of aryl aliphatic glycolipids	Geotrichum sp. F0401B	Otto et al. (2000)
	Formation of citronellol laurate	CAL-B from Candida antarctica	Ganapati and Piyush (2004)
	Synthesis of single isomer chiral drugs	CAL-B from Candida antarctica	Gotor-Fernandez et al. (2006a)
	Synthesis of nitrogenated compounds	CAL-B from Candida antarctica	Gotor-Fernandez et al. (2006b)
Fine chemical synthesis	Synthesis of optically active esters	CAL-B from Candida antarctica	Anderson et al. (1998)
	Synthesis optically active alcohols	CAL-B from Candida antarctica	Rotticci et al. (2001)
	Synthesis of ethyl docosahexaenoate	CAL-B from Candida antarctica	Shimada et al. (2001)
	Ester synthesis	CAL-B from Candida antarctica	Zhang et al. (2003)
	Formation of butyl lactate	CAL-B from Candida antarctica	Pirozzi and Greco (2004)
	Asymmetric synthesis of amino acids/amino esters	CAL-A from Candida antarctica	de Maria et al. (2005)
	Enantioselective esterification of (R)-ketoprofen	CAL-B from Candida antarctica	Ong et al. (2006)
	Organic synthesis of chiral intermediates	CAL-B from Candida antarctica	Gotor-Fernandez et al. (2006a)
Food industry	Formation of butyl caprylate as flavour compound	Pseudomonas fluorescens P38	Tan et al. (1996)
Environmental applications	Bioremediation and bioaugumentation	Acinetobacter sp. 6	Suzuki et al. (2001)
Leather industry	Degreasing using alkaline and acid lipases	Lipases of commercial sources	Afsar and Cetinkaya (2008)
Other applications	Biodiesel synthesis from degummed soybean oil	CAL-B from Candida antarctica	Watanabe et al. (2002)
	Lipase-catalysed biodiesel	CAL-B from Candida antarctica	Chang et al. (2005)

Suzuki T, Nakayama T, Kurihara T, Nishino T, Esaki N. 2001. Cold-active lipolytic activity of psychrotrophic Acinetobacter sp. strain no. 6. J Biosci Bioeng. 92:144–148. doi: 10.1016/S1389-1723(01)80215-2

 PubMed Web of Science ®Google Scholar

Park IH, Kim SH, Lee YS, Lee SC, Zhou Y, Kim CM, Ahn SC, Choi YL. 2009. Gene cloning, purification, and characterization of a cold-adapted lipase produced by Acinetobacter baumannii BD5. J Microbiol Biotechnol. 19:128–135. doi: 10.4014/jmb.0802.130.

 PubMed Web of Science ®Google Scholar

Lee HK, Min JA, Sung HK, Won HS, Byeong CJ. 2003. Purification and characterization of cold active lipase from psychrotrophic Aeromonas sp. LPB4. J Microbiol. 41:22–27.

 Web of Science ®Google Scholar

Imbert M, Gancel F. 2004. Effect of different temperature downshifts on protein synthesis by Aeromonas hydrophila. Curr Microbiol. 49:79–83. doi: 10.1007/s00284-004-4277-8

 PubMed Web of Science ®Google Scholar

Seo JB, Kim HS, Jung GY, Nam MH, Chung JH, Kim JY, Yoo JS, Kim CW, Kwon O. 2004. Psychrophilicity of Bacillus psychrosaccharolyticus: a proteomic study. Proteomics. 4:3654–3659. doi: 10.1002/pmic.200401025

 PubMed Web of Science ®Google Scholar

Joseph B, Ramteke PW. 2013. Extracellular solvent stable cold active lipase from psychrotrophic Bacillus sphaericus MTCC 7526: partial purification and characterization. Ann Microbiol. 63:363–370. doi: 10.1007/s13213-012-0483-y

 Web of Science ®Google Scholar

Do H, Lee JH, Kwon MH, Song HE, An JY, Eom SH, Lee SG, Kim HJ. 2013. Purification, characterization and preliminary X-ray diffraction analysis of a cold-active lipase (CpsLip) from the psychrophilic bacterium Colwellia psychrerythraea 34H. Acta Crystallogr, Sect F: Struct Biol Cryst Commun. 69:920–924. doi: 10.1107/S1744309113019428

 PubMedGoogle Scholar

Rabus R, Ruepp A, Frickey T, Rattei T, Fartmann B, Stark M, Bauer M, Zibat A, Lombardot T, Becker I, et al. 2004. The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments. Environ Microbiol. 6:887–902. doi: 10.1111/j.1462-2920.2004.00665.x

 PubMed Web of Science ®Google Scholar

Jadhav VV, Pote SS, Yadav A, Shouche YS, Bhadekar RK. 2013. Extracellular cold active lipase from the psychrotrophic Halomonas sp. BRI 8 isolated from the Antarctic sea water. Songklanakarin J Sci Technol. 35:623–630.

 Google Scholar

Yuan D, Lan D, Xin R, Yang B, Wang Y. 2014. Biochemical Properties of a new cold-active mono- and diacylglycerol lipase from marine member Janibacter sp. strain HTCC2649. Int J Mol Sci. 15:10554–10566. doi: 10.3390/ijms150610554

 PubMed Web of Science ®Google Scholar

Joseph B, Upadhyaya S, Ramteke P. 2011. Production of cold-active bacterial lipases through semisolid state fermentation using oil cakes. Enzyme Res. 2011:796407. doi:10.4061/2011/796407.

 PubMedGoogle Scholar

Joshi GK, Kumar S, Tripathi BN, Sharma V. 2006. Production of alkaline lipase by Corynebacterium paurometabolum, MTCC 6841 isolated from Lake Naukuchiatal, Uttaranchal state, India. Curr Microbiol. 52:354–358. doi: 10.1007/s00284-005-0224-6

 PubMed Web of Science ®Google Scholar

Joseph B, Shrivastava N, Ramteke PW. 2012. Extracellular cold-active lipase of Microbacterium luteolum isolated from Gangotri glacier, Western Himalaya: isolation, partial purification and characterization. J Genet Eng Biotechnol. 10:137–144. doi: 10.1016/j.jgeb.2012.02.001

 Google Scholar

Wang Q, Zhang C, Hou Y, Lin X, Shen J, Guan X. 2013. Optimization of cold-active lipase production from psychrophilic bacterium Moritella sp. 2-5-10-1 by statistical experimental methods. Biosci Biotechnol Biochem. 77:17–21. doi: 10.1271/bbb.120104

 PubMed Web of Science ®Google Scholar

Wei X, Jiang X, Ye L, Yuan S, Chen Z, Wu M, Yu H. 2013. Cloning, expression and characterization of a new enantioselective esterase from a marine bacterium Pelagibacterium halotolerans B2T. J Mol Catal B Enzym. 97:270–277. doi: 10.1016/j.molcatb.2013.09.002

 Web of Science ®Google Scholar

Kim YO, Khosasih V, Nam BH, Lee SJ, Suwanto A, Kim HK. 2012. Gene cloning and catalytic characterization of cold-adapted lipase of Photobacterium sp. MA1-3 isolated from blood clam. J Biosci Bioeng. 114:589–595. doi: 10.1016/j.jbiosc.2012.06.013

 PubMed Web of Science ®Google Scholar

Seo HJ, Bae SS, Yang SH, Lee JH, Kim SJ. 2005. Photobacterium aplysiae sp. nov., a lipolytic marine bacterium isolated from eggs of the sea hare Aplysia kurodai. Int J Syst Evol Microbiol. 55:2293–2296. doi: 10.1099/ijs.0.63765-0

 PubMed Web of Science ®Google Scholar

Ryu HS, Kim HK, Choi WC, Kim MH, Park SY, Han NS, Oh TK, Lee JK. 2006. New cold-adapted lipase from Photobacterium lipolyticum sp. nov. that is closely related to filamentous fungal lipases. Appl Microbiol Biotechnol. 70:321–326. doi: 10.1007/s00253-005-0058-y

 PubMed Web of Science ®Google Scholar

Park Y-D, Baik KS, Seong CN, Bae KS, Kim S, Chun J. 2006. Photobacterium ganghwense sp. nov., a halophilic bacterium isolated from sea water. Int J Syst Evol Microbiol. 56:745–749. doi: 10.1099/ijs.0.63811-0

 PubMed Web of Science ®Google Scholar

Srinivas TNR, Vijaya Bhaskar Y, Bhumika V, Anil Kumar P. 2013. Photobacterium marinum sp. nov., a marine bacterium isolated from a sediment sample from Palk Bay, India. Syst Appl Microbiol. 36:160–165. doi: 10.1016/j.syapm.2012.12.002

 PubMed Web of Science ®Google Scholar

Zeng X, Xiao X, Wang P, Wang F. 2004. Screening and characterization of psychrotrophic lipolytic bacteria from deep-sea sediments. J Microbiol Biotechnol. 14:952–958.

 Web of Science ®Google Scholar

Lo Giudice A, Michaud L, de Pascale D, De Domenico M, di Prisco G, Fani R, Bruni V. 2006. Lipolytic activity of Antarctic cold adapted marine bacteria. J Appl Microbiol. 101:1039–1048. doi: 10.1111/j.1365-2672.2006.03006.x

 PubMed Web of Science ®Google Scholar

de Pascale D, Cusano AM, Autore F, Parrilli E, di Prisco G, Marino G, Tutino ML. 2008. The cold-active Lip1 lipase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 is a member of a new bacterial lipolytic enzyme family. Extremophiles. 12:311–323. doi: 10.1007/s00792-008-0163-9

 PubMed Web of Science ®Google Scholar

Reddy GSN, Matsumoto GI, Schumann P, Stackebrandt E, Shivaji S. 2004. Psychrophilic pseudomonads from Antarctica: pseudomonas antarctica sp. nov., Pseudomonas meridiana sp. nov. and Pseudomonas proteolytica sp. nov. Int J Syst Evol Microbiol. 54:713–719. doi: 10.1099/ijs.0.02827-0

 PubMed Web of Science ®Google Scholar

Preuss J, Kaiser I, Gehring U. 2001. Molecular characterization of a phosphatidylcholine –hydrolyzing phospholipase C. Eur J Biochem. 268:5081–5091. doi: 10.1046/j.0014-2956.2001.02440.x

 PubMedGoogle Scholar

Leonov SL. 2010. Screening for novel cold-active lipases from wild type bacteria isolates. Innov Rom Food Biotechnol. 6:12–17.

 Google Scholar

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. doi: 10.1046/j.1432-1033.2002.03012.x

 PubMedGoogle Scholar

Muryoi N, Sato M, Kaneko S, Kawahara H, Obata H, Yaish MWF, Griffith M, Glick BR. 2004. Cloning and expression of afpA, a gene encoding an antifreeze protein from the arctic plant growth-promoting rhizobacterium Pseudomonas putida GR12-2. J Bacteriol. 186:5661–5671. doi: 10.1128/JB.186.17.5661-5671.2004

 PubMed Web of Science ®Google Scholar

Kiran GS, Shanmughapriya S, Jayalakshmi J, Selvin J, Gandhimathi R, Sivaramakrishnan S, Arunkumar M, Thangavelu T, Natarajaseenivasan K. 2008. Optimization of extracellular psychrophilic alkaline lipase produced by marine Pseudomonas sp. (MSI057). Bioprocess Biosyst Eng. 31:483–492. doi: 10.1007/s00449-007-0186-0

 PubMed Web of Science ®Google Scholar

Bofill C, Prim N, Mormeneo M, Manresa A, Javier Pastor FI, Diaz P. 2010. Differential behaviour of Pseudomonas sp. 42A2 LipC, a lipase showing greater versatility than its counterpart LipA. Biochimie. 92:307–316. doi: 10.1016/j.biochi.2009.11.005

 PubMed Web of Science ®Google Scholar

Kavitha M, Shanthi C. 2013. Isolation and characterization of cold active lipase producing Pseudomonas sp. 4 from marine samples of Tamilnadu coast. Res J Biotech. 8:57–62.

 Web of Science ®Google Scholar

Ali MSM, Fuzi SFM, Ganasen M, Rahman RNZRA, Basri M, Salleh AB. 2013. Structural adaptation of cold-active RTX lipase from Pseudomonas sp. strain AMS8 revealed via homology and molecular dynamics simulation approaches. Biomed Res Int. 2013:925373. doi: 10.1155/2013/134914.

 PubMed Web of Science ®Google Scholar

Rashid N, Shimada Y, Ezaki S, Atomi H, Imanaka T. 2001. Low-temperature lipase from psychrotrophic Pseudomonas sp. strain KB700A. Appl Environ Microbiol. 67:4064–4069. doi: 10.1128/AEM.67.9.4064-4069.2001

 PubMed Web of Science ®Google Scholar

Novototskaya-Vlasova KA, Petrovskaya LE, Rivkina EM, Dolgikh DA, Kirpichnikov MP. 2013. Characterization of a Cold active lipase from Psychrobacter cryohalolentis K5T and its deletion mutants. Biochemistry (Moscow). 78:385–394. doi: 10.1134/S000629791304007X

 PubMed Web of Science ®Google Scholar

Yumoto I, Hirota K, Sogabe Y, Nodasaka Y, Yokota Y, Hoshino T. 2003. Psychrobacter okhotskensis sp., nov., a lipase-producing facultative psychrophile isolated from the coast of the Okhotsk Sea. Int J Syst Evol Microbiol. 53:1985–1989. doi: 10.1099/ijs.0.02686-0

 PubMed Web of Science ®Google Scholar

Kulakovaa L, Galkina A, Nakayamab T, Nishinob T, Esakia N. 2004. Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly Pro substitution near the active site on its catalytic activity and stability. Biochim Biophys Acta. 1696:59–65. doi: 10.1016/j.bbapap.2003.09.008

 PubMed Web of Science ®Google Scholar

Jinwei Z, Lin S, Zeng R. 2007. Cloning, expression and characterization of a cold-adapted lipase gene from an Antarctic deep-sea psychrotrophic bacterium, Psychrobacter sp. 7195. J Microbiol Biotechnol. 17:604–610.

 PubMed Web of Science ®Google Scholar

Parra LP, Reyes F, Acevedo JP, Salaza O, Andrews BA, Asenjo JA. 2008. Cloning and fusion expression of a cold-active lipase from marine Antarctic origin. Enzyme Microb Technol. 42:371–377. doi: 10.1016/j.enzmictec.2007.11.003

 Web of Science ®Google Scholar

Xuezheng L, Shuoshuo C, Guoying X, Shuai W, Ning D, Jihong S. 2010. Cloning and heterologous expression of two cold-active lipases from the Antarctic bacterium Psychrobacter sp. G. Polar Res. 29:421–429. doi: 10.1111/j.1751-8369.2010.00189.x

 Web of Science ®Google Scholar

De Santi C, Tutino ML, Mandrich L, Giuliani M, Parrilli E, Del Vecchio P, de Pascale D. 2010. The hormone-sensitive lipase from Psychrobacter sp. TA144: new insight in the structural/functional characterization. Biochimie. 92:949–957. doi: 10.1016/j.biochi.2010.04.001

 PubMed Web of Science ®Google Scholar

Chen R, Guo L, Dang H. 2010. Gene cloning, expression and characterization of a cold-adapted lipase from a psychrophilic deep-sea bacterium Psychrobacter sp. C18. World J Microbiol Biotechnol. 27:431–441. doi: 10.1007/s11274-010-0475-7

 Web of Science ®Google Scholar

Abdou AM. 2003. Purification and partial characterization of psychrotrophic Serratia marcescens lipase. J Dairy Sci. 86:127–132. doi: 10.3168/jds.S0022-0302(03)73591-7

 PubMed Web of Science ®Google Scholar

Suzuki Y, Haruki M, Takano K, Morikawa M, Kanaya S. 2004. Possible involvement of an FKBP family member protein from a psychrotrophic bacterium Shewanella sp. SIB1 in cold-adaptation. Eur J Biochem. 271:1372–1381. doi: 10.1111/j.1432-1033.2004.04049.x

 PubMedGoogle Scholar

Joseph B, Ramteke PW, Kumar PA. 2006. Studies on the enhanced production of extracellular lipase by Staphylococcus epidermidis. J Gen Appl Microbiol. 52:315–320. doi: 10.2323/jgam.52.315

 PubMed Web of Science ®Google Scholar

Li M, Yang LR, Xu G, Wu JP. 2013. Screening, purification and characterization of a novel cold-active and organic solvent-tolerant lipase from Stenotrophomonas maltophilia CGMCC 4254. Bioresour Technol. 148:114–120. doi: 10.1016/j.biortech.2013.08.101

 PubMed Web of Science ®Google Scholar

Shieh WY, Chen YW, Chaw SM, Chiu HH. 2003. Vibrio ruber sp. nov., a red, facultatively anaerobic, marine bacterium isolated from sea water. Int J Syst Evol Microbiol. 53:479–484. doi: 10.1099/ijs.0.02307-0

 PubMed Web of Science ®Google Scholar

Mayordomo I, Randez-Gil F, Prieto JA. 2000. Isolation, purification, and characterization of a cold active lipase from Aspergillus nidulans. J Agric Food Chem. 48:105–109. doi: 10.1021/jf9903354

 PubMed Web of Science ®Google Scholar

Patkar SA, Bjorking F, Zundai M, Schulein M, Svendsen A, Heldt-Hansen HP, Gormsen E. 1993. Purification of two lipases from Candida antarctica and their inhibition by various inhibitors. Ind J Chem. 32B:76–80.

 Google Scholar

Uppenberg J, Patkar S, Bergfors T, Jones TA. 1994b. Crystallization and preliminary X-ray studies of lipase B from Candida antarctica. J Mol Biol. 235:790–792. doi: 10.1006/jmbi.1994.1035

 PubMed Web of Science ®Google Scholar

Uppenberg J, Hansen MT, Patkar S, Jones TA. 1994a. The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure. 2:293–308. doi: 10.1016/S0969-2126(00)00031-9

 PubMed Web of Science ®Google Scholar

Zhang N, Suen WC, Windsor W, Xiao L, Madison V, Zaks A. 2003. Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution. Prot Eng. 16:599–605. doi: 10.1093/protein/gzg074

 PubMedGoogle Scholar

Siddiqui KS, Cavicchioli R. 2005. Improved thermal stability and activity in the cold-adapted lipase B from Candida Antarctica following chemical modification with oxidized polysaccharides. Extremophiles. 9:471–476. doi: 10.1007/s00792-005-0464-1

 PubMed Web of Science ®Google Scholar

Lan DM, Yang N, Wang WK, Shen YF, Yang B, Wang YH. 2011. A novel cold-active lipase from Candida albicans: cloning, expression and characterization of the recombinant enzyme. Int J Mol Sci. 12:3950–3965. doi: 10.3390/ijms12063950

 PubMed Web of Science ®Google Scholar

Florczaka T, Daroch M, Wilkinson MC, Białkowska A, Bates AD, Turkiewicz M, Iwanejko LA. 2013. Purification, characterisation and expression in Saccharomyces cerevisiae of LipG7 an enantioselective, cold-adapted lipase from the Antarctic filamentous fungus Geomyces sp. P7 with unusual thermostability characteristics. Enzyme Microb Tech. 53:18–24. doi: 10.1016/j.enzmictec.2013.03.021

 PubMed Web of Science ®Google Scholar

Cai Y, Wang L, Liao X, Ding Y, Sun J. 2009. Purification and partial characterization of two new cold-adapted lipases from mesophilic Geotrichum sp. SYBC WU-3. Process Biochem. 44:786–790. doi: 10.1016/j.procbio.2009.03.011

 Web of Science ®Google Scholar

Kim HR, Hou CT, Lee KT, Kim BH, Kim IH. 2010. Enzymatic synthesis of structured lipids using a novel cold-active lipase from Pichia lynferdii NRRL Y-7723. Food Chem. 122:846–849. doi: 10.1016/j.foodchem.2010.03.067

 Web of Science ®Google Scholar

Smidt H, Fischer A, Fischer P, Schmid RD. 1996. Preparation of optically pure chiral amines by lipase catalyzed enantioselective hydrolysis of N-acyl-amines. Biotechnol Tech. 10:335–338. doi: 10.1007/BF00173249

 Google Scholar

Otto Y, Sawamoto T, Hasuo M. 2000. Tributyrin specifically induces a lipase with a preference for the sn-2 position of triglyceride in Geotrichum sp. F0401B. Biosci Biotechnol Biochem. 64:2497–2499. doi: 10.1271/bbb.64.2497

 PubMed Web of Science ®Google Scholar

Ganapati DY, Piyush SL. 2005. Lipase catalyzed transesterification of methyl acetoacetate with n-butanol. J Mol Cat B Enzy. 32:107–113. doi: 10.1016/j.molcatb.2004.10.003

 Web of Science ®Google Scholar

Gotor-Fernandez V, Brieva R, Gotor V. 2006a. Lipases: useful biocatalysts for the preparation of pharmaceuticals. J Mol Catal B Enzym. 40:111–120. doi: 10.1016/j.molcatb.2006.02.010

 Web of Science ®Google Scholar

Gotor-Fernandez V, Busto E, Gotor V. 2006b. Candida antarctica lipase B: an ideal biocatalyst for the preparation of nitrogenated organic compounds. Adv Synth Catal. 348:797–812. doi: 10.1002/adsc.200606057

 Web of Science ®Google Scholar

Anderson EM, Larsson KM, Kirk O. 1998. One biocatalyst – many applications: the use of Candida antarctica B-lipase in organic synthesis. Biocatal Biotransfor. 16:181–204. doi: 10.3109/10242429809003198

 Web of Science ®Google Scholar

Rotticci D, Ottosson J, Norin T, Hult K. 2001. Candida antarctica lipase B: a tool for the preparation of optically active alcohols. Methods in Biotechnol. 15:261–276.

 Google Scholar

Shimada Y, Watanabe Y, Sugihara A, Baba T, Ooguri T, Moriyama S, Terai T, Tominaga Y. 2001. Ethyl esterification of docosahexaenoic acid in an organic solvent-free system with immobilized Candida antarctica lipase. J Biosci Bioeng. 92:19–23. doi: 10.1016/S1389-1723(01)80192-4

 PubMed Web of Science ®Google Scholar

Pirozzi D, Greco GJ. 2004. Activity and stability of lipases in the synthesis of butyl lactate. Enzym Microb Technol. 34:94–100. doi: 10.1016/j.enzmictec.2003.01.002

 Web of Science ®Google Scholar

de Maria PD, Carboni-Oerlemans C, Tuin B, Bargeman G, van der Meer A, van Gemert R. 2005. Biotechnological applications of Candida antarctica lipase A: state-of-the-art. J Mol Catal, B Enzym. 37:36–46. doi: 10.1016/j.molcatb.2005.09.001

 Web of Science ®Google Scholar

Ong AL, Kamaruddin AH, Bhatia SW, Long WS, Lim ST, Kumari R. 2006. Performance of free Candida antarctica lipase B in the enantioselective esterification of (R)-ketoprofen. Enzyme Microb Technol. 39:924–929. doi: 10.1016/j.enzmictec.2006.01.029

 Web of Science ®Google Scholar

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. doi: 10.1016/0308-8146(95)00243-X

 Web of Science ®Google Scholar

Afsar A, Cetinkaya F. 2008. A research on increasing the effectiveness of degreasing process by using enzymes. Tekstil Ve Konfeksiyon. 18:278–283.

 Web of Science ®Google Scholar

Watanabe Y, Shimada Y, Sugihara A, Tominaga Y. 2002. Conversion of degummed soybean oil to biodiesel fuel with immobilized Candida antarctica lipase. J Mol Catal B Enzy. 17:151–155. doi: 10.1016/S1381-1177(02)00022-X

 Web of Science ®Google Scholar

Chang HM, Liao HF, Lee CC, Shieh CJ. 2005. Optimized synthesis of lipase-catalyzed biodiesel by Novozym 435. J Chem Tech Biotech. 80:307–312. doi: 10.1002/jctb.1166

 Web of Science ®Google Scholar