Properties of Selected Hemicellulases of a Multi-Enzymatic System from Penicillium funiculosum

概要

論文の詳細を見る
A multi-enzymatic system from Penicillium funiculosum displayed α-L-arabinofuranosidase, endo-1,4-β-D-xylanase, β-D-xylosidase and endo-1,3-1,4-β-D-glucanase activities at high levels over a wide acidic pH range of 2.0 to 5.5. Moreover, the pH stability was particularly extended over the wide range of pH of 2.0 to 8.0 with endo-1,3-1,4-β-D-glucanase and endo-1,4-β-D-xylanase; however, α-L-arabinofuranosidase and β-D-xylosidase exhibited higher stability in the pH range of 2.0 to 5.5. The results indicate that the optimal temperature of α-L-arabinofuranosidase (65 °C) and β-D-xylosidase (70 °C) as well as their thermal stability were higher than those of endo-1,3-1,4-β-D-glucanase (60 °C) and endo-1,4-β-D-xylanase (50 °C). Although Vmaxapp of β-D-xylosidase and endo-1,4-β-D-xylanase was higher than that of α-L-arabinofuranosidase and endo-1,3-1,4-β-D-glucanase, respectively, their catalytic efficiency was lower. High levels of ferulolyl esterase, α-D-galactosidase, β-D-mannosidase and endo-1,4-β-D-mannanase activities were also detected in the multi-enzymatic system. The overall features of the multi-enzymatic system from P. funiculosum reveal its potential for degrading and modifying plant cell walls from a variety of food and feedstuffs.
社団法人日本農芸化学会の論文
2009-06-23