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Acta Phys. -Chim. Sin.  2010, Vol. 26 Issue (04): 1113-1118    DOI: 10.3866/PKU.WHXB20100448
BIOPHYSICAL CHEMISTRY     
Adsorptive Immobilization of Four Proteases on Different Molecular Sieves
LIU Ping, XING Guo-Wen, LI Xuan-Wen, YE Yun-Hua
Beijing National Laboratory for Molecular Science, Key Laboratory of Bioorganic Chemistry and Molecular Engineering, Ministry of Education, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, P. R. China
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Abstract  

The immobilization of four different proteases on a series of molecular sieves, including microporous HY, NaY, NH4Y, MCM-22, Hβ zeolites, modified Y zeolites HDAY, HNH4DAY, and mesoporous MCM-41, by adsorption was systematically investigated. The four proteases were α-chymotrypsin, papain, subtilisin, and thermoase (or its pure form thermolysin). The results showed that the enzyme loading amount and the activity of immobilized enzyme were significantly affected not only by the structures and textures of molecular sieves and the enzyme properties, but also by the adsorptive conditions such as buffer pH values and enzyme concentration. In most cases, the amount of protease loading on molecular sieves was relatively higher at pH 6.0, but declined with further increasing of pH values. The nature of the interaction between protease and molecular sieves is discussed. As for α-chymotrypsin, its loading amount on Hβ zeolites was found to be the highest, whereas the activity of α-chymotrypsin immobilized on MCM-22 was the highest, which is probably due to different adsorption states.



Key wordsAdsorption      Immobilization      Protease      Zeolite      Molecular sieve      Peptide synthesis     
Received: 30 November 2009      Published: 17 March 2010
MSC2000:  O647  
Corresponding Authors: YE Yun-Hua     E-mail: yhye@pku.edu.cn
Cite this article:

LIU Ping, XING Guo-Wen, LI Xuan-Wen, YE Yun-Hua. Adsorptive Immobilization of Four Proteases on Different Molecular Sieves. Acta Phys. -Chim. Sin., 2010, 26(04): 1113-1118.

URL:

http://www.whxb.pku.edu.cn/10.3866/PKU.WHXB20100448     OR     http://www.whxb.pku.edu.cn/Y2010/V26/I04/1113

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