Microbial lipases: emerging biocatalysts.

2016 ◽  
pp. 478-488
Author(s):  
S Kanika ◽  
S Naveen ◽  
R Madhu
Keyword(s):  
Microbial Lipases

Industrial biotransformations catalyzed by microbial lipases: screening platform and commercial aspects

2021 ◽  
Author(s):  
María Belén Abdulhamid ◽  
Luciana Costas ◽  
Flavia del Valle Loto ◽  
Mario Domingo Baigorí ◽  
Licia María Pera
Keyword(s):  
Microbial Lipases ◽  
Screening Platform

Microbial lipases: Propitious biocatalysts for the food industry

2021 ◽  
pp. 101509
Author(s):  
Cleonice Aparecida Salgado ◽  
Clarissa Isabela Aparecida dos Santos ◽  
Maria Cristina Dantas Vanetti
Keyword(s):  
Food Industry ◽  
Microbial Lipases

Biodiesel and the Potential Role of Microbial Lipases in Its Production

2019 ◽  
pp. 83-99
Author(s):  
Abhishek Sharma ◽  
Shadiya ◽  
Tanvi Sharma ◽  
Rakesh Kumar ◽  
Khemraj Meena ◽  
...  
Keyword(s):  
Potential Role ◽  
Microbial Lipases

ChemInform Abstract: Solvent Engineering Modulates Stereoselectivity of Microbial Lipases

ChemInform ◽  
2000 ◽  
Vol 31 (39) ◽  
pp. no-no ◽  
Author(s):  
Enrico Cernia ◽  
Cleofe Palocci ◽  
Simonetta Soro
Keyword(s):  
Solvent Engineering ◽  
Microbial Lipases

Technical methods to improve yield, activity and stability in the development of microbial lipases

2010 ◽  
Vol 62 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Zheng-Yu Shu ◽  
Huan Jiang ◽  
Rui-Feng Lin ◽  
Yong-Mei Jiang ◽  
Lin Lin ◽  
...  
Keyword(s):  
Microbial Lipases

Discordant results for determinations of triglycerides in pig sera

1993 ◽  
Vol 39 (1) ◽  
pp. 125-128 ◽  
Author(s):  
T Tuten ◽  
K A Robinson ◽  
D S Sgoutas
Keyword(s):  
Gas Liquid Chromatography ◽  
Glycerol Phosphate ◽  
Serum Triglycerides ◽  
Lipolytic Enzymes ◽  
Chemical Hydrolysis ◽  
Human Sera ◽  
Microbial Lipases ◽  
Sample Method ◽  
Hydrolysis Of ◽  
Enzymatic Methods

Abstract We recently determined triglyceride concentrations in pig sera by three fully enzymatic methods (Kodak Ektachem 700, Hitachi 707, and Abbott EPx) and obtained significantly lower values than those obtained with chemical or enzymatic methods based on chemical hydrolysis. All methods used involve microbial lipases for liberating glycerol from glycerides and glycerol phosphate dehydrogenases or oxidases for subsequent oxidation. The methods were validated against reference methods by using fresh human sera and survey materials. The discordant results were not from matrix sample-method interaction but from incomplete hydrolysis of pig serum triglycerides by the lipolytic enzymes. When serum triglycerides from 10 pigs showing the highest biases were hydrolyzed by microbial lipases and the reaction mixture was subjected to thin-layer and gas-liquid chromatography, the predominant end products were palmitoyl monoglyceride and a mixture of free fatty acids with the following composition (fatty acid as percent of total +/- SD): 16:0, 7.8 +/- 2; 18:0, 5.4 +/- 2.2; 18:1, 53 +/- 12; 18:2, 31 +/- 4.6; and 18:3, 2.5 +/- 1. Assuming that the lipases exhibit the usual specificity toward the 1 and 3 positions of the triglyceride, the data suggest that, in pig, triglycerides 18:1 and 18:2 occupy the 1 and 3 positions and 16:0 (palmitic acid) predominantly occupies the 2 position. Triglycerides of this structure may not be well hydrolyzed by the typical lipolytic enzymes in clinical assays.

On the role of higher plant and microbial lipases in the ruminal hydrolysis of grass lipids

1977 ◽  
Vol 38 (2) ◽  
pp. 225-232 ◽  
Author(s):  
R. M. C. Dawson ◽  
N. Hemington ◽  
G. P. Hazlewood
Keyword(s):  
Rumen Fluid ◽  
Higher Plant ◽  
Microbial Enzymes ◽  
Heat Treated ◽  
Ruminal Degradation ◽  
Complex Lipids ◽  
Microbial Lipases ◽  
Micro Organisms ◽  
Hydrolysis Of

1. The galactolipids of heat-treated, 14C-labelled rye grass S24 administered intraruminally to a sheep fed on an autoclaved diet were rapidly catabolized.2. When grass was homogenized with rumen contents devoid of higher plant lipases the grass galactolipids were rapidly metabolized, but were not metabolized when the rumen contents were boiled to destroy microbial galactolipases.3. 14C-labelled monogalactosyldiglyceride, digalactosyldiglyceride and triolein were metabolized, with the release of 14C-labelled fatty acids when incubated with a homogenate (100 g/l) of grass or clover in rumen fluid from a starved sheep, but not when the rumen fluid was heat-treated to destroy microbial enzymes.4. It is concluded that in the sheep the lipases of rumen micro-organisms play a major part in the ruminal degradation of ingested complex lipids of pasture.

scholarly journals Understanding Structural Features of Microbial Lipases–-An Overview

2008 ◽  
Vol 3 ◽  
pp. ACI.S551 ◽  
Author(s):  
John Geraldine Sandana Mala ◽  
Satoru Takeuchi
Keyword(s):  
Structural Analysis ◽  
Candida Rugosa ◽  
Structural Data ◽  
Data Bank ◽  
Candida Rugosa Lipase ◽  
Structural Features ◽  
X Ray Crystallography ◽  
Versatile Tool ◽  
Microbial Lipases

The structural elucidations of microbial lipases have been of prime interest since the 1980s. Knowledge of structural features plays an important role in designing and engineering lipases for specific purposes. Significant structural data have been presented for few microbial lipases, while, there is still a structure-deficit, that is, most lipase structures are yet to be resolved. A search for ‘lipase structure’ in the RCSB Protein Data Bank ( http://www.rcsb.org/pdb/ ) returns only 93 hits (as of September 2007) and, the NCBI database ( http://www.ncbi.nlm.nih.gov ) reports 89 lipase structures as compared to 14719 core nucleotide records. It is therefore worthwhile to consider investigations on the structural analysis of microbial lipases. This review is intended to provide a collection of resources on the instrumental, chemical and bioinformatics approaches for structure analyses. X-ray crystallography is a versatile tool for the structural biochemists and is been exploited till today. The chemical methods of recent interests include molecular modeling and combinatorial designs. Bioinformatics has surged striking interests in protein structural analysis with the advent of innumerable tools. Furthermore, a literature platform of the structural elucidations so far investigated has been presented with detailed descriptions as applicable to microbial lipases. A case study of Candida rugosa lipase (CRL) has also been discussed which highlights important structural features also common to most lipases. A general profile of lipase has been vividly described with an overview of lipase research reviewed in the past.

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