Progress and Application of Cold-active Protease

doi:10.13523/j.cb.2207051

China Biotechnology

2023, Vol. 43

Issue (1): 115-126 DOI: 10.13523/j.cb.2207051

Progress and Application of Cold-active Protease

HAO Man,SHI Chao-shuo,HUI Wei,LI Xiang-xun,ZHANG Tong-tong,LIU Fu-feng,LU Fu-ping,ZHANG Hui-tu^**(

)

College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China

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Abstract

Cold-active protease is a kind of hydrolytic enzyme that can hydrolyze large proteins into small peptides or amino acids at low temperatures. It is generally produced by microorganisms living at low temperatures and has high catalytic activity at lower ambient temperatures. Therefore, it can avoid waste of resources caused by the rise in temperature in the application process and the special requirements for equipment, and shows unique advantages and commercial value in the application fields of washing, food processing and medical treatment. In this paper, different kinds and sources of microbial cryopinases are reviewed, and their catalytic properties, structural characteristics, current application and future development prospects are analyzed and summarized based on existing research results, aiming to promote the development and application of new cryopinases.

Key words： Cold-active protease Microorganism Catalytic property Architectural feature Industrial application

Received: 25 July 2022 Published: 14 February 2023

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	Hui-tu ZHANG

Cite this article:

HAO Man, SHI Chao-shuo, HUI Wei, LI Xiang-xun, ZHANG Tong-tong, LIU Fu-feng, LU Fu-ping, ZHANG Hui-tu. Progress and Application of Cold-active Protease. China Biotechnology, 2023, 43(1): 115-126.

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https://manu60.magtech.com.cn/biotech/10.13523/j.cb.2207051 OR https://manu60.magtech.com.cn/biotech/Y2023/V43/I1/115

Fig.1 Research flow of cold-active protease

Fig.2 Microorganism producing cold-active protease

Table 1 The catalytic properties of cold-active protease

Fig.3 Subtilisin S41 structure

Table 2 Alignment of cold-active protease structure

Fig.4 Structural comparison of four cold-active proteases (a) Four cold-active proteases polymer chains (b) Complete structure diagram of four cold-active proteases

Fig.5 Methods for de novo protein design^[66] (a) Protein sequence space diagram (b) Protein structure prediction, fixed frame design and design from scratch methods

Table 3 Application of cold-active protease


[1]	Razzaq A, Shamsi S, Ali A, et al. Microbial proteases applications. Frontiers in Bioengineering and Biotechnology, 2019, 7: 110. doi: 10.3389/fbioe.2019.00110 pmid: 31263696

[2]	Kasana R C. Proteases from psychrotrophs: an overview. Critical Reviews in Microbiology, 2010, 36(2): 134-145. doi: 10.3109/10408410903485525 pmid: 20047457

[3]	Bezerra V H S, Cardoso S L, Fonseca-Bazzo Y, et al. Protease produced by endophytic fungi: a systematic review. Molecules, 2021, 26(22): 7062. doi: 10.3390/molecules26227062

[4]	Al-Maqtari Q A, Al-Ansi W, Mahdi A A. Cold-active enzymes and their applications in industrial fields-a review. International Journal of Research in Agricultural Sciences, 2019, 6(4): 2348-3997.

[5]	陈秀兰, 张玉忠, 高培基. 适冷微生物及其适冷机制研究进展. 中国生物工程杂志, 2003, 23(2): 86-90.

[5]	Chen X L, Zhang Y Z, Gao P J. Progress in cold-adapted microorganisms and their cold-adapted mechanism. China Biotechnology, 2003, 23(2): 86-90.

[6]	Nakajima M, Mizusawa K, Yoshida F. Purification and properties of an extracellular proteinase of psychrophilic Escherichia freundii. European Journal of Biochemistry, 1974, 44(1): 87-96. pmid: 4212288

[7]	Kim E H, Cho K H, Lee Y M, et al. Diversity of cold-active protease-producing bacteria from arctic terrestrial and marine environments revealed by enrichment culture. Journal of Microbiology (Seoul, Korea), 2010, 48(4): 426-432.

[8]	Kim D, Park H J, Lee Y M, et al. Screening for cold-active protease-producing bacteria from the culture collection of polar microorganisms and characterization of proteolytic activities. The Korean Joural of Microbiology, 2010, 46(1): 73-79.

[9]	Yadav A N, Sachan S G, Verma P, et al. Cold active hydrolytic enzymes production by psychrotrophic Bacilli isolated from three sub-glacial lakes of NW Indian Himalayas. Journal of Basic Microbiology, 2016, 56(3): 294-307. doi: 10.1002/jobm.201500230 pmid: 26933936

[10]	Olivera N L, Sequeiros C, Nievas M L. Diversity and enzyme properties of protease-producing bacteria isolated from sub-Antarctic sediments of Isla de Los Estados, Argentina. Extremophiles: Life Under Extreme Conditions, 2007, 11(3): 517-526. doi: 10.1007/s00792-007-0064-3

[11]	de Gobba C, Tompa G, Otte J. Bioactive peptides from caseins released by cold active proteolytic enzymes from Arsukibacterium ikkense. Food Chemistry, 2014, 165: 205-215. doi: 10.1016/j.foodchem.2014.05.082

[12]	Hao J H, Sun M. Purification and characterization of a cold alkaline protease from a psychrophilic Pseudomonas aeruginosa HY1215. Applied Biochemistry and Biotechnology, 2015, 175(2): 715-722. doi: 10.1007/s12010-014-1315-2

[13]	Mykytczuk N C S, Foote S J, Omelon C R, et al. Bacterial growth at -15℃; molecular insights from the permafrost bacterium Planococcus halocryophilus Or1. The ISME Journal, 2013, 7(6): 1211-1226. doi: 10.1038/ismej.2013.8

[14]	Han S J, Park H, Kim S, et al. Enhanced production of protease by Pseudoalteromonas arctica PAMC 21717 via statistical optimization of mineral components and fed-batch fermentation. Preparative Biochemistry & Biotechnology, 2016, 46(4): 328-335.

[15]	权淑静, 马焕, 刘德海, 等. 产低温蛋白酶海洋菌筛选、鉴定及性质的初步研究. 河南科学, 2017, 35(1): 78-82.

[15]	Quan S J, Ma H, Liu D H, et al. Screening and enzymatic properties of cold-active protease marine strain. Henan Science, 2017, 35(1): 78-82.

[16]	Mageswari A, Subramanian P, Chandrasekaran S, et al. Systematic functional analysis and application of a cold-active serine protease from a novel Chryseobacterium sp. Food Chemistry, 2017, 217: 18-27. doi: 10.1016/j.foodchem.2016.08.064

[17]	Pereira J Q, Ambrosini A, Passaglia L M P, et al. A new cold-adapted serine peptidase from Antarctic Lysobacter sp. A03: insights about enzyme activity at low temperatures. International Journal of Biological Macromolecules, 2017, 103: 854-862. doi: 10.1016/j.ijbiomac.2017.05.142

[18]	Furhan J, Awasthi P, Sharma S. Biochemical characterization and homology modelling of cold-active alkophilic protease from Northwestern Himalayas and its application in detergent industry. Biocatalysis and Agricultural Biotechnology, 2019, 17: 726-735. doi: 10.1016/j.bcab.2019.01.028

[19]	Damare S, Raghukumar C, Muraleedharan U D, et al. Deep-sea fungi as a source of alkaline and cold-tolerant proteases. Enzyme and Microbial Technology, 2006, 39(2): 172-181. doi: 10.1016/j.enzmictec.2006.03.032

[20]	Papagianni M, Sergelidis D. Purification and biochemical characterization of a novel alkaline protease produced by Penicillium nalgiovense. Applied Biochemistry and Biotechnology, 2014, 172(8): 3926-3938. doi: 10.1007/s12010-014-0824-3 pmid: 24585382

[21]	Gao B, He L, Wei D Z, et al. Identification and magnetic immobilization of a pyrophilous aspartic protease from Antarctic psychrophilic fungus. Journal of Food Biochemistry, 2018, 42(6): e12691. doi: 10.1111/jfbc.12691

[22]	Białkowska A M, Szulczewska K M, Krysiak J, et al. Genetic and biochemical characterization of yeasts isolated from Antarctic soil samples. Polar Biology, 2017, 40(9): 1787-1803. doi: 10.1007/s00300-017-2102-7

[23]	姜春宇, 张媱, 孙燕飞, 等. 产低温蛋白酶酵母菌株的筛选及发酵培养基优化. 中国酿造, 2018, 37(11): 45-50.

[23]	Jiang C Y, Zhang Y, Sun Y F, et al. Screening of low-temperature protease-producing yeast and optimization of fermentation medium. China Brewing, 2018, 37(11): 45-50.

[24]	Białkowska A M, Krysiak J, Florczak T, et al. The psychrotrophic yeast Sporobolomyces roseus LOCK 1119 as a source of a highly active aspartic protease for the in vitro production of antioxidant peptides. Biotechnology and Applied Biochemistry, 2018, 65(5): 726-738. doi: 10.1002/bab.1656 pmid: 29569743

[25]	Daskaya-Dikmen C, Karbancioglu-Guler F, Ozcelik B. Cold active pectinase, amylase and protease production by yeast isolates obtained from environmental samples. Extremophiles: Life Under Extreme Conditions, 2018, 22(4): 599-606. doi: 10.1007/s00792-018-1020-0

[26]	Zhang H T, Mu H Y, Mo Q S, et al. Gene cloning, expression and characterization of a novel cold-adapted protease from Planococcus sp. Journal of Molecular Catalysis B: Enzymatic, 2016, 130: 1-8. doi: 10.1016/j.molcatb.2016.04.002

[27]	Wang Q F, Hou Y H, Xu Z, et al. Optimization of cold-active protease production by the psychrophilic bacterium Colwellia sp. NJ 341 with response surface methodology. Bioresource Technology, 2008, 99(6): 1926-1931. doi: 10.1016/j.biortech.2007.03.028

[28]	潘延云, 张贺迎, 周艳芬, 等. 原生质体融合构建高产碱性蛋白酶工程菌. 应用与环境生物学报, 2002, 8(4): 422-426.

[28]	Pan Y Y, Zhang H Y, Zhou Y F, et al. Construction of engineering strain producing with alkaline protease protoplast fusion. Chinese Journal of Applied and Environmental Biology, 2002, 8(4): 422-426.

[29]	张晓燕. 产低温蛋白酶菌株的筛选及酶学特性研究. 乌鲁木齐: 新疆农业大学, 2014.

[29]	Zhang X Y. Screening of strains producing low temperature protease and study on the enzymatic characteristics of this enzyme. Urumqi: Xinjiang Agricultural University, 2014.

[30]	朱非, 王珊, 周培瑾. 低温酶冷适应的分子机制及其在生物技术中的应用. 微生物学报, 2002, 42(5): 640-644.

[30]	Zhu F, Wang S, Zhou P J. Molecular mechanisms of cold-adapted enzymes to cold environment and their application in biotechnology industry. Acta Microbiologica Sinica, 2002, 42(5): 640-644.

[31]	Joshi G K, Kumar S, Sharma V. Production of moderately halotolerant, SDS stable alkaline protease from Bacillus cereus MTCC 6840 isolated from lake Nainital, Uttaranchal state, India. Brazilian Journal of Microbiology, 2007, 38(4): 773-779. doi: 10.1590/S1517-83822007000400034

[32]	Alam S I, Dube S, Agarwal M K, et al. Purification and characterization of an extracellular protease produced by psychrotolerant Clostridium sp. LP3 from lake sediment of Leh, India. Canadian Journal of Microbiology, 2006, 52(12): 1238-1246. doi: 10.1139/w06-089

[33]	Ray M K, Devi K U, Kumar G S, et al. Extracellular protease from the Antarctic yeast Candida humicola. Applied and Environmental Microbiology, 1992, 58(6): 1918-1923. doi: 10.1128/aem.58.6.1918-1923.1992 pmid: 1622266

[34]	Alam S I, Dube S, Reddy G S N, et al. Purification and characterisation of extracellular protease produced by Clostridium sp. from schirmacher oasis, Antarctica. Enzyme and Microbial Technology, 2005, 36(5-6): 824-831. doi: 10.1016/j.enzmictec.2005.01.011

[35]	Huston A L, Methe B, Deming J W. Purification, characterization, and sequencing of an extracellular cold-active aminopeptidase produced by marine psychrophile Colwellia psychrerythraea strain 34H. Applied and Environmental Microbiology, 2004, 70(6): 3321-3328. doi: 10.1128/AEM.70.6.3321-3328.2004

[36]	Patel T R, Jackman D M, Bartlett F M. Heat-stable protease from Pseudomonas fluorescens T16: purification by affinity column chromatography and characterization. Applied and Environmental Microbiology, 1983, 46(2): 333-337. doi: 10.1128/aem.46.2.333-337.1983 pmid: 6414369

[37]	Hamamoto T, Kaneda M, Horikoshi K, et al. Characterization of a protease from a psychrotroph, Pseudomonas fluorescens 114. Applied and Environmental Microbiology, 1994, 60(10): 3878-3880. doi: 10.1128/aem.60.10.3878-3880.1994 pmid: 16349422

[38]	Hamamoto T. Characterization of a protease from psychrophilic Vibrio sp. strain 5709. Journal of Marine Biotechnology, 1995, 2: 219-222.

[39]	Suzuki S, Odagami T. Low-temperature-active thiol protease from marine bacterium Alteromonas haloplanktis. The Journal of Marine Biotechnology, 1997, 5(4): 230-233.

[40]	Morita Y, Hasan Q, Sakaguchi T, et al. Properties of a cold-active protease from psychrotrophic Flavobacterium balustinum P104. Applied Microbiology and Biotechnology, 1998, 50(6): 669-675. doi: 10.1007/s002530051349 pmid: 9891929

[41]	Oh K H, Seong C S, Lee S W, et al. Isolation of a psychrotrophic Azospirillum sp. and characterization of its extracellular protease. FEMS Microbiology Letters, 1999, 174(1): 173-178. pmid: 10234836

[42]	Turkiewicz M, Pazgier M, Kalinowska H, et al. A cold-adapted extracellular serine proteinase of the yeast Leucosporidium antarcticum. Extremophiles, 2003, 7(6): 435-442. pmid: 12845553

[43]	Secades P, Alvarez B, Guijarro J A. Purification and properties of a new psychrophilic metalloprotease (Fpp2) in the fish pathogen Flavobacterium psychrophilum. FEMS Microbiology Letters, 2003, 226(2): 273-279. pmid: 14553922

[44]	Tondo E C, Lakus F R, Oliveira F A, et al. Identification of heat stable protease of Klebsiella oxytoca isolated from raw milk. Letters in Applied Microbiology, 2004, 38(2): 146-150. pmid: 14746547

[45]	Wang Q F, Miao J L, Hou Y H, et al. Purification and characterization of an extracellular cold-active serine protease from the psychrophilic bacterium Colwellia sp. NJ341. Biotechnology Letters, 2005, 27(16): 1195-1198. doi: 10.1007/s10529-005-0016-x

[46]	Kasana R C, Yadav S K. Isolation of a psychrotrophic Exiguobacterium sp. SKPB 5 (MTCC 7803) and characterization of its alkaline protease. Current Microbiology, 2007, 54(3): 224-229. doi: 10.1007/s00284-006-0402-1

[47]	Kuddus M, Ramteke P W. A cold-active extracellular metalloprotease from Curtobacterium luteum (MTCC 7529): enzyme production and characterization. The Journal of General and Applied Microbiology, 2008, 54(6): 385-392. doi: 10.2323/jgam.54.385

[48]	Kredics L, Terecskei K, Antal Z, et al. Purification and preliminary characterization of a cold-adapted extracellular proteinase from Trichoderma atroviride. Acta Biologica Hungarica, 2008, 59(2): 259-268. doi: 10.1556/ABiol.59.2008.2.11 pmid: 18637564

[49]	Yang C Y, Wang F, Hao J H, et al. Identification of a proteolytic bacterium, HW08, and characterization of its extracellular cold-active alkaline metalloprotease Ps5. Bioscience, Biotechnology, and Biochemistry, 2010, 74(6): 1220-1225. doi: 10.1271/bbb.100011

[50]	Tariq A L, Reyaz A L, Prabakaran J J. Purification and characterization of 56 KDa cold active protease from Serratia marcescens. African Journal of Microbiology Research, 2011, 5(32): 5841-5847.

[51]	Kuddus M, Ramteke P W. Production optimization of an extracellular cold-active alkaline protease from Stenotrophomonas maltophilia MTCC 7528 and its application in detergent industry. African Journal of Microbiology Research, 2011, 5(7): 809-816. doi: 10.5897/AJMR10.806

[52]	Park I, Cho J. Production of an extracellular protease by an Antarctic bacterial isolate (Bacillus sp. JSP1) as a potential feed additive. Revista Colombiana de Ciencias Pecuarias, 2011, 24(1): 3-10.

[53]	Saba I, Qazi P H, Rather S A, et al. Purification and characterization of a cold active alkaline protease from Stenotrophomonas sp., isolated from Kashmir, India. World Journal of Microbiology & Biotechnology, 2012, 28(3): 1071-1079. doi: 10.1007/s11274-011-0905-1

[54]	Salwan R, Kasana R C. Purification and characterization of an extracellular low temperature-active and alkaline stable peptidase from psychrotrophic Acinetobacter sp. MN 12 MTCC (10786). Indian Journal of Microbiology, 2013, 53(1): 63-69. doi: 10.1007/s12088-012-0344-1 pmid: 24426080

[55]	Yang J, Li J, Mai Z M, et al. Purification, characterization, and gene cloning of a cold-adapted thermolysin-like protease from Halobacillus sp. SCSIO 20089. Journal of Bioscience and Bioengineering, 2013, 115(6): 628-632. doi: 10.1016/j.jbiosc.2012.12.013

[56]	Chen K, Mo Q S, Liu H, et al. Identification and characterization of a novel cold-tolerant extracellular protease from Planococcus sp. CGMCC 8088. Extremophiles: Life Under Extreme Conditions, 2018, 22(3): 473-484. doi: 10.1007/s00792-018-1010-2

[57]	Park H J, Lee C W, Kim D, et al. Crystal structure of a cold-active protease (Pro21717) from the psychrophilic bacterium, Pseudoalteromonas arctica PAMC 21717, at 1.4 Å resolution: structural adaptations to cold and functional analysis of a laundry detergent enzyme. PLoS One, 2018, 13(2): e0191740. doi: 10.1371/journal.pone.0191740

[58]	Rueda M, Ferrer-Costa C, Meyer T, et al. A consensus view of protein dynamics. Proceedings of the National Academy of Sciences of the United States of America, 2007, 104(3): 796-801.

[59]	Kuddus M, Arif J M, Ramteke P W. Structural adaptation and biocatalytic prospective of microbial cold-active α-amylase. African Journal of Microbiology Research, 2012, 6(2): 206-213.

[60]	Al-Ghanayem A A, Joseph B. Current prospective in using cold-active enzymes as eco-friendly detergent additive. Applied Microbiology and Biotechnology, 2020, 104(7): 2871-2882. doi: 10.1007/s00253-020-10429-x pmid: 32037467

[61]	Gatti-Lafranconi P, Natalello A, Rehm S, et al. Evolution of stability in a cold-active enzyme elicits specificity relaxation and highlights substrate-related effects on temperature adaptation. Journal of Molecular Biology, 2010, 395(1): 155-166. doi: 10.1016/j.jmb.2009.10.026 pmid: 19850050

[62]	Davail S, Feller G, Narinx E, et al. Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the Antarctic psychrophile Bacillus TA41. Journal of Biological Chemistry, 1994, 269(26): 17448-17453. pmid: 8021248

[63]	莫清珊. 新型低温蛋白酶基因的克隆表达及酶学性质研究. 天津: 天津科技大学, 2014.

[63]	Mo Q S. Gene cloning, expression and characterization of novel cold-adapted proteases. Tianjin: Tianjin University of Science & Technology, 2014.

[64]	周冠宇, 李江华, 彭政, 等. 定点突变提高枯草芽孢杆菌角蛋白酶的低温催化活性. 微生物学通报, 2022, 49(1): 1-13.

[64]	Zhou G Y, Li J H, Peng Z, et al. Improving the low-temperature activity of Bacillus subtilis keratinase by site-directed mutagenesis. Microbiology China, 2022, 49(1): 1-13.

[65]	王朋辉, 王伟贤, 曾晖, 等. 碱性蛋白酶洗涤稳定性提高的研究进展. 日用化学工业, 2022, 52(2): 180-189.

[65]	Wang P H, Wang W X, Zeng H, et al. Research progress in improving the washing performance of alkaline protease. China Surfactant Detergent & Cosmetics, 2022, 52(2): 180-189.

[66]	Huang P S, Boyken S E, Baker D. The coming of age of de novo protein design. Nature, 2016, 537(7620): 320-327. doi: 10.1038/nature19946

[67]	王雄健. 洗涤剂用蛋白酶的发酵及造粒技术研究. 太原: 山西大学, 2018.

[67]	Wang X J. Study on fermentation and granulation technology of detergent protease. Taiyuan: Shanxi University, 2018.

[68]	Joshi S, Satyanarayana T. Biotechnology of cold-active proteases. Biology, 2013, 2(2): 755-783. doi: 10.3390/biology2020755

[69]	Park H J, Han S J, Yim J H, et al. Characterization of an Antarctic alkaline protease, a cold-active enzyme for laundry detergents. Korean Journal of Microbiology, 2018, 54(1): 60-68.

[70]	周晶, 袁丽, 高瑞昌. 产低温蛋白酶动性球菌的筛选及其在低盐鱼露发酵中的应用. 食品科学, 2021, 42(8): 122-128.

[70]	Zhou J, Yuan L, Gao R C. Screening of low-temperature protease-producing Planococcus and its application in low-salt fish sauce fermentation. Food Science, 2021, 42(8): 122-128.

[71]	陈飞, 吴生文, 张志刚. 蛋白酶在酒类生产中的应用现状. 酿酒科技, 2011, 199(1): 82-84.

[71]	Chen F, Wu S W, Zhang Z G. Present status of the application of protease in wine production. Liquor-making Science & Technology, 2011, 199(1): 82-84.

[72]	宋常欣, 陈玲. 啤酒非生物稳定剂的应用和比较. 食品与发酵工业, 2001, 27(4): 79-81.

[72]	Song C X, Chen L. Application and comparison of abiotic stabilizers for beer. Food and Fermentation Industries, 2001, 27(4): 79-81.

[73]	Hamid B, Mohiddin F A. Cold-active enzymes in food processing. Enzymes in Food Technology, 2018, 19: 383-400.

[74]	张春鸽. 细菌低温蛋白酶及其在海参活性物质提取中的初步研究. 哈尔滨: 哈尔滨工业大学, 2013.

[74]	Zhang C G. Low temperautre bacteria proteasa and its preliminary study on extraction of sea cucumber active substances. Harbin: Harbin Institute of Technology, 2013.

[75]	Adam M, Potter A S, Potter S S. Psychrophilic proteases dramatically reduce single-cell RNA-seq artifacts: a molecular atlas of kidney development. Development (Cambridge, England), 2017, 144(19): 3625-3632.

[76]	Craik C S, Page M J, Madison E L. Proteases as therapeutics. The Biochemical Journal, 2011, 435(1): 1-16. doi: 10.1042/BJ20100965

[77]	Mekkes J R, le Poole I C, Das P K, et al. Efficient debridement of necrotic wounds using proteolytic enzymes derived from Antarctic krill: a double-blind, placebo-controlled study in a standardized animal wound model. Wound Repair and Regeneration, 1998, 6(1): 50-57. pmid: 9776850

[78]	Hellgren K. Krill enzymes (Krillase®) an important factor to improve oral hygiene. Oral Health Care - Pediatric, Research, Epidemiology and Clinical Practices, 2012. DOI: 10.5772/22056. doi: 10.5772/22056

[79]	Hilmarsson H, Stefansson B, Bjarnason J B, et al. Virucidal activities of penzyme against herpes simplex veiru type 1 (poster 928). European Cooperation in Science and Technology, 2010, 928: 2-4.

[80]	Moran A J, Hills M, Gunton J, et al. Heat-labile proteases in molecular biology applications. FEMS Microbiology Letters, 2001, 197(1): 59-63. pmid: 11287147

[81]	Furhan J, Salaria N, Jabeen M, et al. Partial purification and characterisation of cold-active metalloprotease by Bacillus sp. AP 1 from Apharwat peak, Kashmir. Pakistan Journal of Biotechnology, 2019, 16(1): 47-54. doi: 10.34016/pjbt.2019.16.1.8

[82]	Baghel V S, Tripathi R D, Ramteke P W, et al. Psychrotrophic proteolytic bacteria from cold environment of Gangotri glacier, Western Himalaya, India. Enzyme and Microbial Technology, 2005, 36(5-6): 654-659. doi: 10.1016/j.enzmictec.2004.09.005

[83]	Yuan Q Z, Hayashi A, Kitamura Y, et al. Purification and characterization of cold-adapted metalloprotease from deep sea water lactic acid bacteria Enterococcus faecalis TN-9. International Journal of Biology, 2009, 1(2): 12.

[84]	Tamaki H, Hanada S, Kamagata Y, et al. Flavobacterium limicola sp. nov., a psychrophilic, organic-polymer-degrading bacterium isolated from freshwater sediments. International Journal of Systematic and Evolutionary Microbiology, 2003, 53(Pt 2): 519-526. doi: 10.1099/ijs.0.02369-0

[85]	Margesin R, Dieplinger H, Hofmann J, et al. A cold-active extracellular metalloprotease from Pedobacter cryoconitis-production and properties. Research in Microbiology, 2005, 156(4): 499-505. pmid: 15862448

[86]	郝建华, 刘均忠, 王芳, 等. 海洋低温蛋白酶MP去除人发鳞质层的研究. 毛纺科技, 2013, 41(2): 6-10.

[86]	Hao J H, Liu J Z, Wang F, et al. Study of removinging npophysis layer of hair with marine cold-adapted protease MP. Wool Textile Journal, 2013, 41(2): 6-10.

[87]	He H L, Chen X L, Li J W, et al. Taste improvement of refrigerated meat treated with cold-adapted protease. Food Chemistry, 2004, 84(2): 307-311. doi: 10.1016/S0308-8146(03)00242-5

[88]	Zambare V, Nilegaonkar S, Kanekar P. A novel extracellular protease from Pseudomonas aeruginosa MCM B-327: enzyme production and its partial characterization. New Biotechnology, 2011, 28(2): 173-181. doi: 10.1016/j.nbt.2010.10.002

[89]	Turkiewicz M, Gromek E, Kalinowska H, et al. Biosynthesis and properties of an extracellular metalloprotease from the Antarctic marine bacterium Sphingomonas paucimobilis. Journal of Biotechnology, 1999, 70(1-3): 53-60. doi: 10.1016/S0168-1656(99)00057-7

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