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中国生物工程杂志

China Biotechnology
China Biotechnology  2011, Vol. 31 Issue (10): 45-49    DOI:
    
Chemical Modification of Savinase by Dextran and Its Enzyme Properties
ZHU Yi-ran, FAN Xue-rong, WANG Qiang, CHEN Ren-ren, YU Yuan-yuan, YUAN Jiu-gang
Jiangnan University Key Laboratory of Eco-Textiles, Ministry of Education, Wuxi 214122, China
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Abstract  

Savinase was chemically modified using NaIO4 oxidised dextran. The molecular size and the secondary structure of modified Savinase were characterized by GPC and CD. The factors related with the activity of the modified Savinase, such as kinetic constant, temperature and pH value were studied and compared with those of native Savinase. GPC results showed that the molecular size of the protease increased after chemical modification. CD spectra revealed the difference between native and modified Savinase, which further demonstrated the conjugate of oxidized dextran and Savinase. Compared with the native Savinase, the modified one had a higher affinity to casein. The optimum reaction temperature for both of the protease was 40℃, and the modified Savinase had a better thermal stability at 30℃~50℃. The stability of modified Savinase is better than the native one at pH8.5~9.5.



Key wordsSavinase      Dextran      Chemical modification      Molecular size     
Received: 29 April 2011      Published: 25 October 2011
ZTFLH:  Q556  
Cite this article:

ZHU Yi-ran, FAN Xue-rong, WANG Qiang, CHEN Ren-ren, YU Yuan-yuan, YUAN Jiu-gang. Chemical Modification of Savinase by Dextran and Its Enzyme Properties. China Biotechnology, 2011, 31(10): 45-49.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2011/V31/I10/45


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