Characterization of cellulose acetate micropore membrane immobilized acylase I.
This paper describes an innovative method for the immobilization of acylase I, which was entrapped into the CA-CTA micropore membrane. The most suitable casting solutions proportion for immobilizing the enzyme was obtained through orthogonal experiment. Properties of the enzyme membrane were investigated and compared with those of free enzyme and blank membrane. The thermal stability and pH stability of the enzyme inside the membrane were changed by immobilization. The optimum pH was found to be 6.0, which changes 1.0 unit compared with that of free acylase I. The optimum temperature was found to be about 90 degrees C, which is higher than that of free acylase I (60 degrees C). Experimental results showed that immobilization had effects on the kinetic parameters of acylase I.
Guo
Yong-Sheng
YS
Department of Chemistry, Zhejiang University, Hangzhou 310027, China.
Wang
Jie
J
Song
Xi-Jin
XJ
D000327:Adsorption; D000581:Amidohydrolases / Q000032:analysis / Q000737:chemistry* / Q000648:ultrastructure*; D002482:Cellulose / Q000031:analogs & derivatives* / Q000737:chemistry*; D020099:Coated Materials, Biocompatible / Q000737:chemistry*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008422:Materials Testing; D008567:Membranes, Artificial; D008851:Micropore Filters; D016062:Porosity; D013696:Temperature
D020099:Coated Materials, Biocompatible; D004800:Enzymes, Immobilized; D008567:Membranes, Artificial; C005062:acetylcellulose; D002482:Cellulose; D000581:Amidohydrolases; C019672:aminoacylase I