NDLI: α-Chymotrypsin Catalyzed Hydrolysis of N-Benzoyl-L-Tyrosine Ethyl Ester Anchored in β-Cyclodextrin

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α-Chymotrypsin Catalyzed Hydrolysis of N-Benzoyl-L-Tyrosine Ethyl Ester Anchored in β-Cyclodextrin

Content Provider	Scilit
Author	Kumble, Sandeep Prabhu Ramadoss, Candadai S.
Copyright Year	1995
Description	N-Benzoyl-L-tyrosine ethyl ester, a substrate for α-chymotrypsin (EC. 3.4.21.1) was solubilised by β-cyclodextrin at a molar ratio of 1.0:2.0 but not by α-cyclodextrin. The completely water soluble BTEE-β-cyclodextrin complex served as an excellent substrate for the enzyme α-chymotrypsin. The rate of hydrolysis of such a cyclodextrin anchored BTEE was identical to that of the substrate in Triton X-100 micelles, but was higher than the methanol solubilised substrate. The pH-activity profile was similar for all the three substrate preparations. The specificity constant (kcat/Km) was higher in the case of BTEE-β-cyclodextrin compared to the methanol and Triton X-100 solubilised substrates. However, the enthalpy of activation was found to be increased in the case of Triton X-100 and β-cyclodextrin anchored substrates.
Related Links	http://www.tandfonline.com/doi/pdf/10.3109/10242429509003190
Ending Page	291
Page Count	11
Starting Page	281
ISSN	10242422
e-ISSN	10292446
DOI	10.3109/10242429509003190
Journal	Biocatalysis and Biotransformation
Issue Number	4
Volume Number	12
Language	English
Publisher	Informa UK Limited
Publisher Date	1995-01-01
Access Restriction	Open
Subject Keyword	Journal: Biocatalysis and Biotransformation Textiles Cyclodextrin Chymotrypsin Catalyzed Chymotrypsin Tyrosine Ethyl Ethyl Ester
Content Type	Text
Resource Type	Article
Subject	Biochemistry Catalysis Biotechnology

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