Purification and characterization of haloalkaline thermoactive, solvent stable and SDS-induced protease from Bacillus sp.: a potential additive for laundry detergents.

Abstract:

:An extracellular haloalkaline, thermoactive, solvent stable, SDS-induced serine protease was purified and characterized from an alkali-thermo tolerant strain Bacillus sp. SM2014 isolated from reverse osmosis reject. The enzyme was purified to homogeneity with recovery of 54.4% and purity fold of 64. The purified enzyme was composed of single polypeptide of molecular mass about 71 kDa. The enzyme showed optimum activity at alkaline pH 10 and temperature 60°C. The km and Vmax for the enzyme was 0.57 mg/ml and 445.23 U/ml respectively. The enzyme showed novel catalytic ability at high pH (10), temperature (60°C) and salinity (3M). Moreover, the stability of enzyme in organic solvents (50% v/v) of logP ≥ 2 signified the prospective of this enzyme for peptide synthesis. The compatibility of the enzyme with surfactants and various detergent matrices together with wash performance test confirmed its potential applicability in laundry industry.

journal_name

Bioresour Technol

journal_title

Bioresource technology

authors

Jain D,Pancha I,Mishra SK,Shrivastav A,Mishra S

doi

10.1016/j.biortech.2011.10.081

subject

Has Abstract

pub_date

2012-07-01 00:00:00

pages

228-36

eissn

0960-8524

issn

1873-2976

pii

S0960-8524(11)01569-0

journal_volume

115

pub_type

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