scholarly journals High-yield purification of an organic solvent-tolerant lipase from Pseudomonas sp. strain S5

2005 ◽  
Vol 341 (2) ◽  
pp. 267-274 ◽  
Author(s):  
Raja Noor Zaliha R.A. Rahman ◽  
Syarul Nataqain Baharum ◽  
Mahiran Basri ◽  
Abu Bakar Salleh
Keyword(s):  
Organic Solvent ◽  
High Yield ◽  
Pseudomonas Sp ◽  
Organic Solvent Tolerant ◽  
Solvent Tolerant

scholarly journals New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica

2019 ◽  
Vol 20 (6) ◽  
pp. 1264 ◽  
Author(s):  
Leelatulasi Salwoom ◽  
Raja Raja Abd. Rahman ◽  
Abu Salleh ◽  
Fairolniza Mohd. Shariff ◽  
Peter Convey ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Organic Solvents ◽  
Rice Bran Oil ◽  
Lipolytic Activity ◽  
Pseudomonas Sp ◽  
Lipase Gene ◽  
Cold Adapted ◽  
Organic Solvent Tolerant ◽  
Wide Range ◽  
Solvent Tolerant

In recent years, studies on psychrophilic lipases have become an emerging area of research in the field of enzymology. The study described here focuses on the cold-adapted organic solvent tolerant lipase strain Pseudomonas sp. LSK25 isolated from Signy Station, South Orkney Islands, maritime Antarctic. Strain LSK25 lipase was successfully cloned, sequenced, and over-expressed in an Escherichia coli system. Sequence analysis revealed that the lipase gene of Pseudomonas sp. LSK25 consists of 1432 bp, lacks an N-terminal signal peptide and encodes a mature protein consisting of 476 amino acids. The recombinant LSK25 lipase was purified by single-step purification using Ni-Sepharose affinity chromatography and had a molecular mass of approximately 65 kDa. The final recovery and purification fold were 44% and 1.3, respectively. The LSK25 lipase was optimally active at 30 °C and at pH 6. Stable lipolytic activity was reported between temperatures of 5–30 °C and at pH 6–8. A significant enhancement of lipolytic activity was observed in the presence of Ca2+ ions, the organic lipids of rice bran oil and coconut oil, a synthetic C12 ester and a wide range of water immiscible organic solvents. Overall, lipase strain LSK25 is a potentially desirable candidate for biotechnological application, due to its stability at low temperatures, across a range of pH and in organic solvents.

scholarly journals Organic Solvent-tolerant Lipase from Pseudomonas sp. BCNU 154

2013 ◽  
Vol 23 (10) ◽  
pp. 1246-1251 ◽  
Author(s):  
Hye Jung Choi ◽  
Min Jung Hwang ◽  
Jeoung-Yoon Seo ◽  
Woo Hong Joo
Keyword(s):  
Organic Solvent ◽  
Pseudomonas 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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