

Author: Huo Yanli Li Yue Yuan Zhi Huang Jiaxian
Publisher: Humana Press, Inc
ISSN: 0273-2289
Source: Applied Biochemistry and Biotechnology, Vol.119, Iss.2, 2004-11, pp. : 121-131
Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.
Abstract
Glucoamylase was immobilized onto novel porous polymer supports. The properties of immobilized glucoamylase and the relationship between the activity of immobilized enzyme and the properties of porous polymer supports were investigated. Compared with the native enzyme, the temperature profile of immobilized glucoamylase was widened, and the optimum pH was also changed. The optimum substrate concentration of immobilized glucoamylase was higher than that of native enzyme. After storage for 23 d, the immobilized glucoamylase still maintained about 84% of its initial activity, whereas the native enzyme only maintained about 58% of the initial activity. Moreover, after using repeatedly seven times, the immobilized enzyme maintained about 85% of its initial activity. Furthermore, the properties of porous polymer supports had an effect on the activity of the immobilized glucoamylase.
Related content




Applied Biochemistry and Biotechnology, Vol. 163, Iss. 8, 2011-04 ,pp. :


By Eldin M. Seuror E. Nasr M. Tieama H.
Applied Biochemistry and Biotechnology, Vol. 164, Iss. 1, 2011-05 ,pp. :

