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Purification and characterization of a salt, solvent, detergent and bleach tolerant protease from a new gamma-Proteobacterium isolated from the marine environment of the Sundarbans

Paper ID Volume ID Publish Year Pages File Format Full-Text
36298 45127 2006 8 PDF Available
Title
Purification and characterization of a salt, solvent, detergent and bleach tolerant protease from a new gamma-Proteobacterium isolated from the marine environment of the Sundarbans
Abstract

In this communication we report purification and characterization of a single salt, solvent, detergent and bleach tolerant alkaline serine protease produced by a truly marine bacterium. Based on the 16S rRNA gene sequence, absence of polyhydroxybutyrate accumulation, growth with very high NaCl levels as well as with hydrocarbons as sole carbon source, the isolate was classified as a new bacterium belonging to the gamma-Proteobacteria family. A 69-fold purification (specific activity 791.7 U/mg protein, unit expressed as μmole of tyrosine liberated per minute) was achieved by a three-step purification procedure. The enzyme is active over a broad range of pH (6.0–11.0), the optimum being at 9.0. This protease enzyme shows activity from 30 to 70 °C and Ca2+ increase the thermostability. This enzyme exhibits appreciable activity in presence of up to 30% NaCl and is highly stable even after 18 h pre-incubation with 35% (w/v) NaCl. While Ba2+ and Ca2+ enhance the enzyme activity, heavy metals like Co2+, Zn2+, Hg2+ inactivate the enzyme. The enzyme is completely stable in presence of laboratory detergents (Tween 80 and Triton X-100), oxidizing agents, reducing agents, commercial detergents and bleaches (hydrogen peroxide and sodium perborate) after 1 h of pre-incubation. Water miscible and immiscible organic solvents like ethylene glycol, ethanol, butanol, acetone, DMSO, xylene and perchloroethylene enhance as well as stabilize the enzyme activity.Reflectance measurements during wash performance studies show that our enzyme is capable of almost complete removal of recalcitrant blood and egg stains in both wet and dry wash operations. Enzymatic activity against a wide variety of substrates indicates that our enzyme can be investigated for a range of commercial applications especially for soy protein and gelatin hydrolysis in the food processing industry as well as for the dehairing process in the leather industry in addition to catalyzing hydrolysis reactions at high salt concentrations.

Keywords
Marine bacteria; Serine protease; Gamma-Proteobacteria; Sundarbans
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Purification and characterization of a salt, solvent, detergent and bleach tolerant protease from a new gamma-Proteobacterium isolated from the marine environment of the Sundarbans
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 41, Issue 1, January 2006, Pages 208–215
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us