<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sanatan, Prashant T.</style></author><author><style face="normal" font="default" size="100%">Lomate, Purushottam R.</style></author><author><style face="normal" font="default" size="100%">Giri, Ashok P.</style></author><author><style face="normal" font="default" size="100%">Hivrale, Vandana K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Characterization of a chemostable serine alkaline protease from Periplaneta americana</style></title><secondary-title><style face="normal" font="default" size="100%">BMC Biochemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Chemostability</style></keyword><keyword><style  face="normal" font="default" size="100%">Industrial catalyst</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect proteases</style></keyword><keyword><style  face="normal" font="default" size="100%">Periplaneta americana</style></keyword><keyword><style  face="normal" font="default" size="100%">Serine alkaline protease</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><publisher><style face="normal" font="default" size="100%">BIOMED CENTRAL LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">14</style></volume><pages><style face="normal" font="default" size="100%">32</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Background: Proteases are important enzymes involved in numerous essential physiological processes and hold a strong potential for industrial applications. The proteolytic activity of insects' gut is endowed by many isoforms with diverse properties and specificities. Thus, insect proteases can act as a tool in industrial processes. Results: In the present study, purification and properties of a serine alkaline protease from Periplaneta americana and its potential application as an additive in various bio-formulations are reported. The enzyme was purified near to homogeneity by using acetone precipitation and Sephadex G-100 gel filtration chromatography. Enzyme activity was increased up to 4.2 fold after gel filtration chromatography. The purified enzyme appeared as single protein-band with a molecular mass of similar to 27.8 kDa in SDS-PAGE. The optimum pH and temperature for the proteolytic activity for purified protein were found around pH 8.0 and 60 degrees C respectively. Complete inhibition of the purified enzyme by phenylmethylsulfonyl fluoride confirmed that the protease was of serine-type. The purified enzyme revealed high stability and compatibility towards detergents, oxidizing, reducing, and bleaching agents. In addition, enzyme also showed stability towards organic solvents and commercial detergents. Conclusion: Several important properties of a serine protease from P. Americana were revealed. Moreover, insects can serve as excellent and alternative source of industrially important proteases with unique properties, which can be utilized as additives in detergents, stain removers and other bio-formulations. Properties of the P. americana protease accounted in the present investigation can be exploited further in various industrial processes. As an industrial prospective, identification of enzymes with varying essential properties from different insect species might be good approach and bioresource.&lt;/p&gt;</style></abstract><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.938
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