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An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: Enzyme purification and characterization

Paper ID Volume ID Publish Year Pages File Format Full-Text
18473 42724 2006 8 PDF Available
Title
An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: Enzyme purification and characterization
Abstract

The organic solvent-tolerant strain K protease was purified to homogeneity by ammonium sulphate precipitation and anion exchange chromatography with 124-fold increase in specific activity. The molecular mass of the purified enzyme as revealed by SDS-PAGE electrophoresis is 51,000 Da. The strain K protease was an alkaline metalloprotease with an optimum pH and temperature of 10 and 70 °C, respectively. The enzyme showed stability and activation in the presence of organic solvents with log Pa/w values equal or more than 4.0. After 14 days of incubation, the purified protease was activated 1.11, 1.82, 1.50, 1.75 and 1.80 times in 1-decanol, isooctane, decane, dodecane and hexadecane, respectively.

Keywords
Pseudomonas; Organic solvent-tolerant bacterium; Characterization; Organic solvent-stable enzyme; Alkaline metaloprotease
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An organic solvent-stable alkaline protease from Pseudomonas aeruginosa strain K: Enzyme purification and characterization
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 7, 3 November 2006, Pages 1484–1491
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
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