Open AccessPurification and characterization of the (1→3)‐β‐glucanases from Acremonium sp. IMI 383068
Author(s) -
McDougall Barbara M,
Seviour Robert J
Publication year - 2004
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 - 10.1016/s0378-1097(03)00913-3
Subject(s) - laminarin , biochemistry , extracellular , enzyme , hydrolysis , fungus , peptide sequence , substrate (aquarium) , gene , biology , chemistry , stereochemistry , botany , ecology
Three extracellular (1→3)‐β‐glucanases were purified from the fungus Acremonium sp. IMI 383068. Higher activities were unexpectedly obtained with pustulan, a (1→6)‐β‐glucan as carbon source, than when grown with laminarin, a (1→3)‐β‐glucan. Preliminary evidence suggests that these enzymes are not constitutive, but are inducible, and that their synthesis is repressed by glucose. All three had the same molecular masses, similar pH and temperature optima and none were glycosylated. They all appeared to have an exo‐hydrolytic mode of substrate attack. N‐terminal amino acid sequence data indicate that substantial post‐translational modification of these had occurred, and that while two may be encoded by the same gene, the third may be genetically different.