Open AccessThe 92‐kDa chitinase from Streptomyces olivaceoviridis contains a lysine‐C endoproteinase at its N‐terminus
Author(s) -
Radwan H.H.,
Plattner H.J.,
Menge U.,
Diekmann H.
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07003.x
Subject(s) - chitinase , biochemistry , lysine , actinomycetales , peptide sequence , biology , casein , amino acid , streptomycetaceae , fast protein liquid chromatography , serine , enzyme , molecular mass , streptomyces , chemistry , bacteria , gene , genetics
Serine proteinases of 42, 22 and 14 kDa were purified from the culture fluid of Streptomyces olivaceoviridis by FPLC. The first 14 amino acids at their N‐termini were identical and coincide with the N‐terminal amino acid sequence of 92‐kDa chitinase, which was found to hydrolyse casein. The four proteins hydrolyse synthetic substrates at the carboxyl group of lysine and (more slowly) arginine. The 14‐kDa endoproteinase releases only two fragments of 42 and 43 kDa from β‐galactosidase. When the pure 92‐kDa chitinase was incubated at 37°C in Tris·HCl buffer, it was cleaved into a 70‐kDa chitinase and a 22‐kDa proteinase which in its part is rapidly degraded to a 14‐kDa proteinase.