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 |
| |
Authors: | Peter Bordier H j, Amanda M. Slade, Richard E.H. Wettenhall,Geoffrey B. Fincher |
| |
Affiliation: | Peter Bordier Høj, Amanda M. Slade, Richard E.H. Wettenhall,Geoffrey B. Fincher, |
| |
Abstract: | 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 Mr 32 000, a pI 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 NH2-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. |
| |
Keywords: | (1 → 3)-β-Glucanase Germination Amino acid sequence (Barley) |
本文献已被 ScienceDirect 等数据库收录! |
|