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Isolation and characterization of organic solvent stable protease from alkaliphilic marine <i style="mso-bidi-font-style:normal">Saccharopolyspora </i>species

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Title Isolation and characterization of organic solvent stable protease from alkaliphilic marine Saccharopolyspora species
 
Creator Raut, G R
Chakraborty, S
Chopade, B A
Kokare, C R
 
Subject Alkaliphilic
Saccharopolyspora species
Organic solvent stable
Protease
Salt tolerant
Peptide synthesis
 
Description 131-138
Protease enzyme from thermostable, organic
solvent tolerant and less extensively studied marine Sacccharoplyspora species is reported in the present study. Genus
of the isolated strain was identified as Saccharopolyspora
based on 16S
r-DNA sequencing as well as the morphological characteristics and biochemical
properties. Optimum pH for cell
growth and protease production was pH
10.0. Anionic (SDS) and non-ionic (Tweens) surfactants increased the cell
membrane permeability, therefore enhancing the enzyme production. Proteolytic activity of the supernatant of
the culture was stable in the presence of various organic solvents. Stability
of the enzyme in the presence of organic solvents of the logarithm of the
partition coefficient (log P) was equal to or more than 3.2. Enzyme
retained 98, 97, 95 and 94% of its activity after the incubation in p-xylene,
toluene, n-hexane and n-decane, respectively. Solvent-tolerant microorganism
and the solvent-stable enzyme produced by this novel marine Sacccharoplyspora species can be used as biocatalyst for peptide synthesis in the presence of organic solvents.
 
Date 2013-02-19T13:05:18Z
2013-02-19T13:05:18Z
2013-02
 
Type Article
 
Identifier 0975-1033 (Online); 0379-5136 (Print)
http://hdl.handle.net/123456789/15996
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJMS Vol.42(1) [February 2013]