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Chymotrypsin modified with polyethylene glycol catalyzes peptide synthesis reaction in benzene
Author(s) -
Matsushima Ayako,
Okada Masato,
Inada Yuji
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80615-8
Subject(s) - chemistry , chymotrypsin , phenylalanine , polyethylene glycol , organic chemistry , tyrosine , trypsin , benzene , enzyme , amino acid , biochemistry
Chymotrypsin was modified in the zymogen form with 2,4‐bis( O ‐methoxypolyethylene glycol)‐6‐chloro‐ s ‐triazine (activated PEG 2 ), followed by activation with trypsin. The modified enzyme was soluble in benzene and retained its enzymic activity. Acid‐amide bond formation by the modified enzyme proceeded efficiently in benzene: N ‐benzoyltyrosine butylamide was made from N ‐benzoyl‐L‐tyrosine ethyl ester and n ‐butyl‐amine, and benzoyltyrosine(oligo)phenylalanine ethyl esters were formed from N ‐benzoyl‐L‐tyrosine ethyl ester and L‐phenylalanine ethyl ester.