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.
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