Specificities of α-Chymotrypsin and Subtilisin Carlsberg
نویسندگان
چکیده
منابع مشابه
Acylation of subtilisin Carlsberg by phenyl esters.
Approximate Hammett reaction constants rho calculated from k2/K8 values of several phenyl esters of N-acetyl-L-phenylalanine, hippuric acid, and beta-phenylpropionic acid are 0.0, 0.4, and 1.0 respectively. To determine whether the lack of substituent effect of k2/K8 with the N-acetyl-L-phenylalanine esters is a result of substituent-insensitive k2 or rate-limiting association of enzyme and sub...
متن کاملComparative studies of the specificities of -chymotrypsin and subtilisin BPN'. Studies with flexible and 'locked' substrates.
Subtilisin BPN' hydrolysed N-acetyl-l-3-(2-naphthyl)-alanine methyl ester, N-acetyl-l-leucine methyl ester and N-acetyl-l-valine methyl ester, faster than alpha-chymotrypsin. Of eight ;locked' substrates tested, only methyl 5,6-benzindan-2-carboxylate was hydrolysed faster by subtilisin, whereas the other esters were better substrates for chymotrypsin. Compared with the values for chymotrypsin,...
متن کاملSpecificities of &hymotrypsin and Subtilisin Carl&erg
A study of the comparative specificities of cr-chymotrypsin and subtilisin Carlsberg has been focused mainly on the extent to which a-acetamido groups of some specific and nonspecific activated ester substrates affect the reactivity of each enzyme. Comparisons are based upon k, and k,: K,,, corrected for substrate intrinsic reactivities ((k,), and (k,: K&J. Among p-nitrophenyl P-phenylpropionat...
متن کاملImmobilization of Subtilisin Carlsberg on Modified Silica Gel by Cross-linking and Covalent Binding Methods
Proteases are important enzymes that their role in various industries is undeniable. However, keeping enzymes stable during its activity in harsh conditions is so important. In this study, protease enzyme was immobilized on the porous silica particles and its stability in different temperatures and pHs was evaluated. First silica particles were aminated by 3-aminopropyltriethoxysilane then the ...
متن کاملObtaining higher transesterification rates with subtilisin Carlsberg in nonaqueous media.
Three phase partitioning (protein precipitate obtained as an interfacial layer between lower aqueous and upper t-butanol phases, formed by the addition of ammonium sulphate and t-butanol to the aqueous solution of protein) followed by lyophilization in the presence of two-component excipient resulted in 400-480x increases in transesterification activity of lyophilized powders of subtilisin Carl...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42991-8