Open Accessβ‐Glucosidase from the cellulolytic system of Alternaria alternata autolyzed cultures
Author(s) -
Martínez María Jesús,
Vázquez Covadonga,
Guillén Francisco,
Reyes Fuensanta
Publication year - 1988
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.1574-6968.1988.tb02812.x
Subject(s) - alternaria alternata , enzyme , cellobiose , hydrolysis , biochemistry , alternaria , chemistry , sephadex , chromatography , biology , cellulase , botany
A β‐glucosidase from centrifugated autolyzed cultures of Alternaria alternata has been purified 71 times by Sephadex G‐200, CM‐Biogel A and DEAE‐Biogel A successively. The enzyme is a glycoprotein with 16% sugar and a M r of 160 000, formed by two subunits of 60 000 and 80 000. The enzyme has optimum pH of 5 units and optimum reaction temperature of 50°C, being stable in a pH range of 3–8 and 0 to 60°C. The enzyme hydrolyzes different substrates showing maximum affinity and maximum hydrolysis velocity on cellobiose. The β‐glucosidase is inhibited by gluconolactone but not by 10 mM glucose.