<?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%">Shankar, Shiv</style></author><author><style face="normal" font="default" size="100%">Laxman, Ryali Seeta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Immobilization of conidiobolus coronatus alkaline protease on waste fungal biomass</style></title><secondary-title><style face="normal" font="default" size="100%">Environmental Engineering and Management Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alkaline Protease</style></keyword><keyword><style  face="normal" font="default" size="100%">Conidiobolus coronatus</style></keyword><keyword><style  face="normal" font="default" size="100%">fungal biomass</style></keyword><keyword><style  face="normal" font="default" size="100%">Immobilization</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">11</style></number><publisher><style face="normal" font="default" size="100%">GH ASACHI TECHNICAL UNIV IASI</style></publisher><pub-location><style face="normal" font="default" size="100%">71 MANGERON BLVD, IASI, 700050, ROMANIA</style></pub-location><volume><style face="normal" font="default" size="100%">10</style></volume><pages><style face="normal" font="default" size="100%">1727-1732</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Alkaline protease from Conidiobolus coronatus which is optimally active at pH 10 and 40 degrees C finds application in leather and detergent industries as well as for recovery of silver from waste photographic films. The protease was immobilized in Ca-alginate, polyacrylamide gel and alkali treated waste fungal biomass (ATWFB). ATWFB was found to be most suitable among the matrices tested. Glutaraldehyde marginally increased the binding to ATWFB. Binding of protease to ATWFB seems to be through adsorption as confirmed by FTIR spectra. Though temperature optima of free and immobilized proteases were identical, optimum pH of the immobilized enzyme shifted to 11 from 10. Temperature stability of the protease increased after immobilization. Immobilized protease could be reused 3 times with marginal loss in activity.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">11</style></issue><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">1.004</style></custom4></record></records></xml>