Literature DB >> 15304746

Lipases and their industrial applications: an overview.

Alain Houde1, Ali Kademi, Danielle Leblanc.   

Abstract

Lipases (triacylglycerol acylhydrolase, EC 3.1.1.3) are part of the family of hydrolases that act on carboxylic ester bonds. The physiologic role of lipases is to hydrolyze triglycerides into diglycerides, monoglycerides, fatty acids, and glycerol. These enzymes are widely found throughout the animal and plant kingdoms, as well as in molds and bacteria. Of all known enzymes, lipases have attracted the most scientific attention. In addition to their natural function of hydrolyzing carboxylic ester bonds, lipases can catalyze esterification, interesterification, and transesterification reactions in nonaqueous media. This versatility makes lipases the enzymes of choice for potential applications in the food, detergent, pharmaceutical, leather, textile, cosmetic, and paper industries. The most significant industrial applications of lipases have been mainly found in the food, detergent, and pharmaceutical sectors. Limitations of the industrial use of these enzymes have mainly been owing to their high production costs, which may be overcome by molecular technologies, enabling the production of these enzymes at high levels and in a virtually purified form.

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Year:  2004        PMID: 15304746     DOI: 10.1385/abab:118:1-3:155

Source DB:  PubMed          Journal:  Appl Biochem Biotechnol        ISSN: 0273-2289            Impact factor:   2.926


  58 in total

1.  Efficient secretion of lipase r27RCL in Pichia pastoris by enhancing the disulfide bond formation pathway in the endoplasmic reticulum.

Authors:  Chong Sha; Xiao-Wei Yu; Meng Zhang; Yan Xu
Journal:  J Ind Microbiol Biotechnol       Date:  2013-08-30       Impact factor: 3.346

2.  Directed evolution methods for overcoming trade-offs between protein activity and stability.

Authors:  Samuel D Stimple; Matthew D Smith; Peter M Tessier
Journal:  AIChE J       Date:  2019-10-09       Impact factor: 3.993

3.  Isolation and characterization of a metagenome-derived thermoalkaliphilic esterase with high stability over a broad pH range.

Authors:  Ji-Eun Choi; Min-A Kwon; Hye Young Na; Dae-Hyun Hahm; Jae Kwang Song
Journal:  Extremophiles       Date:  2013-09-13       Impact factor: 2.395

4.  Partial characterization of a crude cold-active lipase from Rhodococcus cercidiphylli BZ22.

Authors:  Dahai Yu; Rosa Margesin
Journal:  Folia Microbiol (Praha)       Date:  2014-04-25       Impact factor: 2.099

5.  Switch of substrate specificity of hyperthermophilic acylaminoacyl peptidase by combination of protein and solvent engineering.

Authors:  Chang Liu; Guangyu Yang; Lie Wu; Guohe Tian; Zuoming Zhang; Yan Feng
Journal:  Protein Cell       Date:  2011-07-12       Impact factor: 14.870

6.  Acceleration of Swiss cheese ripening by microbial lipase without affecting its quality characteristics.

Authors:  Sapna Rani; Sharmili Jagtap
Journal:  J Food Sci Technol       Date:  2018-11-30       Impact factor: 2.701

7.  Copper Ferrite Magnetic Nanoparticles for the Immobilization of Enzyme.

Authors:  Sachin V Otari; Sanjay K S Patel; Sang-Yong Kim; Jung Rim Haw; Vipin C Kalia; In-Won Kim; Jung-Kul Lee
Journal:  Indian J Microbiol       Date:  2018-11-30       Impact factor: 2.461

8.  Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure.

Authors:  Erik M Nordwald; Joseph G Plaks; Jared R Snell; Marcelo C Sousa; Joel L Kaar
Journal:  Chembiochem       Date:  2015-10-14       Impact factor: 3.164

9.  A new cold-adapted, organic solvent stable lipase from mesophilic Staphylococcus epidermidis AT2.

Authors:  Nor Hafizah Ahmad Kamarudin; Raja Noor Zaliha Raja Abd Rahman; Mohd Shukuri Mohamad Ali; Thean Chor Leow; Mahiran Basri; Abu Bakar Salleh
Journal:  Protein J       Date:  2014-06       Impact factor: 2.371

10.  In silico characterization of the global Geobacillus and Parageobacillus secretome.

Authors:  Pedro H Lebre; Habibu Aliyu; Pieter De Maayer; Don A Cowan
Journal:  Microb Cell Fact       Date:  2018-10-03       Impact factor: 5.328

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