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Recombinant microbial lipases for biotechnological applications
Authors:Schmidt-Dannert C
Affiliation:1. Department of Chemical Engineering and Materials Science, University of California, Irvine, Irvine, CA, 92697, United States;2. Department of Electrical and Computer Engineering and Division of Materials Science and Engineering, Boston University, Boston, MA, 02215, United States;1. University of Illinois at Chicago, Chicago, IL 60607, USA;2. University of Central Florida, Orlando, FL 32816, USA;3. Rush University Medical Center, Chicago, IL 60612, USA;4. Nemours Children׳s Hospital, Orlando, FL 32827, USA;1. Department of Endocrine, Shanghai Pudong New Area Gongli Hospital, Shanghai, China;2. Department of Endocrine, The 118th Hospital of Chinese PLA, Wenzhou, Zhejiang, China;1. Department of Science and Technology/National Research Foundation: Vaccine Preventable Diseases, University of the Witwatersrand, Johannesburg, South Africa;2. MRC, Respiratory and Meningeal Pathogens Research Unit, University of the Witwatersrand, Johannesburg, South Africa;3. National Institutes for Communicable Diseases, Johannesburg, South Africa;1. Centre for Infection and Immunity, School of Medicine, Dentistry and Biomedical Sciences, Queen''s University Belfast, Belfast, Northern Ireland, UK;2. CEPR, INSERM U1100/EA6305, University of Tours, Tours, France;3. Our Lady''s Hospital for Sick Children, Dublin, Ireland;4. National Children''s Research Centre, Crumlin, Dublin, Ireland
Abstract:Lipases, mainly of microbial origin, represent the most widely used class of enzymes in biotechnological applications and organic chemistry. Modern methods of genetic engineering combined with an increasing knowledge of structure and function will allow further adaptation to industrial needs and exploration of novel applications. Production of such tailored lipases requires their functional overexpression in a suitable host. Hence, this article describes the functional heterologous production of commercially important microbial lipases. Based on the knowledge of different lipases' substrate binding sites, the most suitable lipase for a particular application may be selected.
Keywords:
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