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《CIESC Journal》 2011-10
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Purification and immobilization of a thermoalkaliphilic catalase from Thermoascus aurantiacus

KE Zunzhu,ZHANG Zhaohui,CHEN Xiaolong(College of Biological and Environmental Engineering,Zhejiang University of Technology,Hangzhou 310014,Zhejiang,China)  
After treating with(NH4)2SO4 fractional precipitation and DEAE-Sepharose anion-exchange column,a thermoalkaliphilic catalase from Thermoascus aurantiacus was purified.The catalase identified by SDS-PAGE was composed of two identical sub-units and had a molecular weight of 1.9×105.The catalase was highly active over a temperature range from 25℃ to 75℃ and a pH range from 7 to 13,having the optimum activity at 75℃ and pH 12.These results demonstrated that the catalase was thermoalkaliphilic.The Km value for the purified catalase was 40.74 mmol·L-1 and the k2 value was 1.59×104 μmol·(min·mg protein)-1.The catalase was immobilized onto chitosan beads by covalent binding.The immobilized catalase showed higher pH stability and thermostability than the free catalase.It retained about 55% of its initial activity after 13 repeated cycles during the total 130 min reaction time.The properties mentioned above showed that this catalase had a potential application in removing residual hydrogen peroxide from bleaching streams in industrial bleaching processes.
【Fund】: 浙江省重点科研工业项目(2006C21117)~~
【CateGory Index】: Q814.2
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