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• W1998101125 endingPage "1292" @default.
• W1998101125 startingPage "1286" @default.
• W1998101125 abstract "A multi-enzymatic system from Penicillium funiculosum displayed alpha-L-arabinofuranosidase, endo-1,4-beta-D-xylanase, beta-D-xylosidase and endo-1,3-1,4-beta-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-beta-D-glucanase and endo-1,4-beta-D-xylanase; however, alpha-L-arabinofuranosidase and beta-D-xylosidase exhibited higher stability in the pH range of 2.0 to 5.5. The results indicate that the optimal temperature of alpha-L-arabinofuranosidase (65 degrees C) and beta-D-xylosidase (70 degrees C) as well as their thermal stability were higher than those of endo-1,3-1,4-beta-D-glucanase (60 degrees C) and endo-1,4-beta-D-xylanase (50 degrees C). Although V(maxapp) of beta-D-xylosidase and endo-1,4-beta-D-xylanase was higher than that of alpha-L-arabinofuranosidase and endo-1,3-1,4-beta-D-glucanase, respectively, their catalytic efficiency was lower. High levels of ferulolyl esterase, alpha-D-galactosidase, beta-D-mannosidase and endo-1,4-beta-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." @default.
• W1998101125 created "2016-06-24" @default.
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• W1998101125 date "2009-06-23" @default.
• W1998101125 modified "2023-09-26" @default.
• W1998101125 title "Properties of Selected Hemicellulases of a Multi-Enzymatic System from<i>Penicillium funiculosum</i>" @default.
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• W1998101125 doi "https://doi.org/10.1271/bbb.80808" @default.
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