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Isolation and characterization of a (1 → 3)‐β‐glucan endohydrolase from germinating barley (Hordeum vulgare) : amino acid sequence similarity with barley (1 → 3, 1 → 4)‐β‐glucanases
Author(s) -
Høj Peter Bordier,
Slade Amanda M.,
Wettenhall Richard E.H.,
Fincher Geoffrey B.
Publication year - 1988
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(88)80643-4
Subject(s) - laminarin , hordeum vulgare , glucanase , glucan , hordeum , amino acid , hydrolysis , biochemistry , biology , enzyme , peptide sequence , avena , chemistry , botany , poaceae , gene
A (1 → 3)‐β‐glucan 3‐glucanohydrolase (EC 3.2.1.39) has been purified approx. 190‐fold from extracts of germinating barley. The enzyme has an apparent M r 32 000, a p I of 8.6, and a pH optimum of 5.6. Analysis of hydrolysis products released from the (1 → 3)‐β‐glucan, laminarin, shows that the enzyme is an endohydrolase. Sequence analysis of the 46 NH 2 ‐terminal amino acids of the (1 → 3)‐β‐glucanase reveals 54% positional identity with barley (1 → 3,1 → 4)‐β‐glucanases (EC 3.2.1.73) and suggests a common evolutionary origin for these two classes of β‐glucan endohydrolases. The barley (1 → 3)‐β‐glucanase also exhibits significant similarity with a (1 → 3)‐β‐glucanase from tobacco.