Abdel Malak C A
Department of Chemistry, Moscow State University, Russia.
Biochem J. 1992 Dec 15;288 ( Pt 3)(Pt 3):941-3. doi: 10.1042/bj2880941.
Calf chymosin was shown to catalyse peptide synthesis optimally over the range pH 4-5, giving satisfactory yields of methyl esters or p-nitroanilides of benzyloxycarbonyl tetra- to hexa-peptides, provided that hydrophobic amino-acid residues form the new peptide bonds. The effectiveness of the enzyme depends also on the nature of adjacent amino-acid residues. As an aspartate-proteinase with a characteristic specificity pattern chymosin would be useful for the synthesis of middle-length peptides.
已证明，小牛凝乳酶在pH 4 - 5范围内能最佳地催化肽合成，对于苄氧羰基四肽至六肽的甲酯或对硝基苯胺，只要疏水性氨基酸残基形成新的肽键，就能获得令人满意的产率。该酶的有效性还取决于相邻氨基酸残基的性质。作为一种具有特征性特异性模式的天冬氨酸蛋白酶，凝乳酶将有助于合成中等长度的肽。
