Isolation and production of organic solvent tolerant protease from bacterial burn infection, Staphylococcus aureus KP091274

Organic solvent-resistant proteases are used to synthesize valuable pharmaceutical and industrial compounds. Using an available and inexpensive source can be very effective in producing this enzyme. For this purpose, Staphylococcus aureus KP091274 was isolated from burn infection and a medium optimization procedure in the presence of organic solvents was considered for four factors of incubation time, the concentration of Mg2+, glycerol and sorbitol using the response surface methodology. The results of this statistical method showed that incubation time has the most effect and glycerol concentration has the least positive effect on enzyme secretion. As a result of applying the optimized conditions in the bacterial culture medium (3mM of Mg2+, 1.5% W/V of glycerol, 0.4% W/V of sorbitol and 72 hours of incubation), the enzyme secretion reaches its maximum.

Download Full-text

Microbial Production of Aliphatic (S)-Epoxyalkanes by Using Rhodococcus sp. Strain ST-10 Styrene Monooxygenase Expressed in Organic-Solvent-Tolerant Kocuria rhizophila DC2201

Applied and Environmental Microbiology ◽

10.1128/aem.03405-14 ◽

2015 ◽

Vol 81 (6) ◽

pp. 1919-1925 ◽

Cited By ~ 23

Author(s):

Hiroshi Toda ◽

Takuya Ohuchi ◽

Ryouta Imae ◽

Nobuya Itoh

Keyword(s):

Organic Solvent ◽

Enantiomeric Excess ◽

Reaction System ◽

Content Type ◽

Styrene Monooxygenase ◽

Organic Solvent Tolerant ◽

Biphasic Reaction ◽

Solvent Tolerant ◽

Optimized Conditions ◽

Kocuria Rhizophila

ABSTRACTWe describe the development of biocatalysis for producing optically pure straight-chain (S)-epoxyalkanes using styrene monooxygenase ofRhodococcussp. strain ST-10 (RhSMO). RhSMO was expressed in the organic solvent-tolerant microorganismKocuria rhizophilaDC2201, and the bioconversion reaction was performed in an organic solvent-water biphasic reaction system. The biocatalytic process enantioselectively converted linear terminal alkenes to their corresponding (S)-epoxyalkanes using glucose and molecular oxygen. When 1-heptene and 6-chloro-1-hexene were used as substrates (400 mM) under optimized conditions, 88.3 mM (S)-1,2-epoxyheptane and 246.5 mM (S)-1,2-epoxy-6-chlorohexane, respectively, accumulated in the organic phase with good enantiomeric excess (ee; 84.2 and 95.5%). The biocatalysis showed broad substrate specificity toward various aliphatic alkenes, including functionalized and unfunctionalized alkenes, with good to excellent ee. Here, we demonstrate that this biocatalytic system is environmentally friendly and useful for producing various enantiopure (S)-epoxyalkanes.

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