Organic Solvent Tolerant Lipases and Applications

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.

Download Full-text

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

Process Biochemistry ◽

10.1016/j.procbio.2012.01.003 ◽

2012 ◽

Vol 47 (4) ◽

pp. 635-642 ◽

Cited By ~ 21

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

Download Full-text

Lipase from organic solvent tolerant Bacillus strain C5: Isolation and Identification

International Journal of Scientific Research ◽

10.15373/22778179/june2013/9 ◽

2012 ◽

Vol 2 (6) ◽

pp. 26-28

Author(s):

B. Rajesh B. Rajesh ◽

◽

I. Bhaskar Reddy

Keyword(s):

Organic Solvent ◽

Isolation And Identification ◽

Bacillus Strain ◽

Organic Solvent Tolerant ◽

Solvent Tolerant

Download Full-text

Gene cloning, overexpression and characterization of a novel organic solvent tolerant and thermostable lipase from Galactomyces geotrichum Y05

Journal of Molecular Catalysis B Enzymatic ◽

10.1016/j.molcatb.2007.07.006 ◽

2007 ◽

Vol 49 (1-4) ◽

pp. 28-35 ◽

Cited By ~ 47

Author(s):

Jinyong Yan ◽

Jiangke Yang ◽

Li Xu ◽

Yunjun Yan

Keyword(s):

Organic Solvent ◽

Gene Cloning ◽

Thermostable Lipase ◽

Organic Solvent Tolerant ◽

Solvent Tolerant

Download Full-text

Optimization of an organic solvent-tolerant lipase production by Staphylococcus capitis SH6. Immobilization for biodiesel production and biodegradation of waste greases

Preparative Biochemistry & Biotechnology ◽

10.1080/10826068.2021.1920034 ◽

2021 ◽

pp. 1-15

Author(s):

Fatma Rmili ◽

Bilel Hadrich ◽

Mohamed Chamkha ◽

Adel Sayari ◽

Ahmed Fendri

Keyword(s):

Organic Solvent ◽

Lipase Production ◽

Biodiesel Production ◽

Staphylococcus Capitis ◽

Organic Solvent Tolerant ◽

Solvent Tolerant

Download Full-text

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

Catalysts ◽

10.3390/catal10010055 ◽

2020 ◽

Vol 10 (1) ◽

pp. 55 ◽

Cited By ~ 3

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.

Download Full-text