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Esterification of N ‐benzyloxycarbonyldipeptides in ethanol–water with immobilized papain
Author(s) -
Kawashiro Katsuhiro,
Ishizaki Hideyuki,
Sugiyama Shigeru,
Hayashi Hiromu
Publication year - 1993
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260420307
Subject(s) - papain , chemistry , amberlite , yield (engineering) , ethanol , chromatography , catalysis , amino acid , peptide , ethyl ester , organic chemistry , enzyme , biochemistry , materials science , adsorption , metallurgy
Abstract The esterification of some N ‐benzyloxycarbonyl ( Z )‐dipeptides in ethanol‐containing water was investigated using papain as a catalyst. The esterification took place in ethanol containing a samll amount of water (2% v/v, pH 9) with free papain at room temperature. The yield (after 24 h) of the ethyl ester was in the range of 25% to 50%. Any peptide bond cleavage of the substrates was not observed during esterification, indicating that the unfavorable amidase activity of papain was well depressed under these conditions. However, dipeptides having a D‐amino amino acid ( Z ‐valyl‐D‐alanine) or a bulky amino acid ( Z ‐valylvaline) at the C ‐terminal position could not be esterified. It was found that the immobilization of papain on Amberlite XAD‐8 increased the yield of the ester significantly as compared with free papain. In the esterification of Z ‐valylalanine using immobilized papain, the optimum water content, pH of an added buffer, and temperature were found to be 2% (v/v), 9, and 40°C, respectively. The water content affected the yield of the product ester significantly.© 1993 John Wiley & Sons, Inc.