An organic solvent–tolerant lipase from Streptomyces sp. CS133 for enzymatic transesterification of vegetable oils in organic media

2012 ◽  
Vol 47 (4) ◽  
pp. 635-642 ◽  
Author(s):  
Poonam Mander ◽  
Seung Sik Cho ◽  
Jaya Ram Simkhada ◽  
Yun Hee Choi ◽  
Da Jeong Park ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Vegetable Oils ◽  
Organic Media ◽  
Streptomyces Sp ◽  
Enzymatic Transesterification ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant

Transesterification of Waste Cooking Oil by an Organic Solvent-Tolerant Alkaline Lipase from Streptomyces sp. CS273

2013 ◽  
Vol 172 (3) ◽  
pp. 1377-1389 ◽  
Author(s):  
Poonam Mander ◽  
Hah-Young Yoo ◽  
Seung Wook Kim ◽  
Yun Hee Choi ◽  
Seung Sik Cho ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Waste Cooking Oil ◽  
Alkaline Lipase ◽  
Streptomyces Sp ◽  
Cooking Oil ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant

scholarly journals Organic Solvent Tolerant Lipases and Applications

2014 ◽  
Vol 2014 ◽  
pp. 1-15 ◽  
Author(s):  
Shivika Sharma ◽  
Shamsher S. Kanwar
Keyword(s):  
Organic Solvent ◽  
Immobilized Lipase ◽  
Industrial Applications ◽  
Fatty Acid Esters ◽  
Reverse Direction ◽  
Organic Media ◽  
Two Phase ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant ◽  
Esterification Reactions

Lipases are a group of enzymes naturally endowed with the property of performing reactions in aqueous as well as organic solvents. The esterification reactions using lipase(s) could be performed in water-restricted organic media as organic solvent(s) not only improve(s) the solubility of substrate and reactant in reaction mixture but also permit(s) the reaction in the reverse direction, and often it is easy to recover the product in organic phase in two-phase equilibrium systems. The use of organic solvent tolerant lipase in organic media has exhibited many advantages: increased activity and stability, regiospecificity and stereoselectivity, higher solubility of substrate, ease of products recovery, and ability to shift the reaction equilibrium toward synthetic direction. Therefore the search for organic solvent tolerant enzymes has been an extensive area of research. A variety of fatty acid esters are now being produced commercially using immobilized lipase in nonaqueous solvents. This review describes the organic tolerance and industrial application of lipases. The main emphasis is to study the nature of organic solvent tolerant lipases. Also, the potential industrial applications that make lipases the biocatalysts of choice for the present and future have been presented.

An organic solvent-tolerant alkaline lipase from Streptomyces sp. CS268 and its application in biodiesel production

2012 ◽  
Vol 17 (1) ◽  
pp. 67-75 ◽  
Author(s):  
Poonam Mander ◽  
Seung Sik Cho ◽  
Jaya Ram Simkhada ◽  
Yun Hee Choi ◽  
Da Jeong Park ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Biodiesel Production ◽  
Alkaline Lipase ◽  
Streptomyces Sp ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant

scholarly journals Biochemical and Structural Characterization of Cross-Linked Enzyme Aggregates (CLEAs) of Organic Solvent Tolerant Protease

Catalysts ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 55 ◽  
Author(s):  
Muhammad Syafiq Mohd Razib ◽  
Raja Noor Zaliha Raja Abd Rahman ◽  
Fairolniza Mohd Shariff ◽  
Mohd Shukuri Mohamad Ali
Keyword(s):  
Structural Analysis ◽  
Organic Solvent ◽  
Average Diameter ◽  
Relative Activity ◽  
Biochemical Properties ◽  
Biochemical Interaction ◽  
Organic Solvent Tolerant ◽  
Random Aggregate ◽  
Solvent Tolerant ◽  
The Stability

Cross-linked enzyme aggregates (CLEAs) is an immobilization technique that can be used to customize enzymes under an optimized condition. Structural analysis on any enzyme treated with a CLEA remains elusive and has been less explored. In the present work, a method for preparing an organic solvent tolerant protease using a CLEA is disclosed and optimized for better biochemical properties, followed by an analysis of the structure of this CLEA-treated protease. The said organic solvent tolerant protease is a metalloprotease known as elastase strain K in which activity of the metalloprotease is measured by a biochemical interaction with azocasein. Results showed that when a glutaraldehyde of 0.02% (v/v) was used under a 2 h treatment, the amount of recovered activity in CLEA-elastase was highest. The recovered activity of CLEA-elastase and CLEA-elastase-SB (which was a CLEA co-aggregated with starch and bovine serum albumin (BSA)) were at an approximate 60% and 80%, respectively. The CLEA immobilization of elastase strain K allowed the stability of the enzyme to be enhanced at high temperature and at a broader pH. Both CLEA-elastase and CLEA-elastase-SB end-products were able to maintain up to 67% enzyme activity at 60 °C and exhibiting an enhanced stability within pH 5–9 with up to 90% recovering activity. By implementing a CLEA on the organic solvent tolerant protease, the characteristics of the organic solvent tolerant were preserved and enhanced with the presence of 25% (v/v) acetonitrile, ethanol, and benzene at 165%, 173%, and 153% relative activity. Structural analysis through SEM and dynamic light scattering (DLS) showed that CLEA-elastase had a random aggregate morphology with an average diameter of 1497 nm.

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