Properties of selected hemicellulases of a multi-enzymatic system from Penicillium funiculosum.
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.
Karboune
Salwa
S
Department of Food Science and Agricultural Chemistry, McGill University, Quebec, Canada.
L'Hocine
Lamia
L
Anthoni
Julie
J
Geraert
Pierre-André
PA
Kermasha
Selim
S
D055162:Biocatalysis; D004795:Enzyme Stability; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010407:Penicillium / Q000201:enzymology*; D013696:Temperature
D006026:Glycoside Hydrolases; C023305:hemicellulase