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A Phanerochaete chrysosporium β-d-glucosidase/β-d-xylosidase with specificity for (1 → 3)-β-d-glucan linkages

✍ Scribed by José L. Copa-Patiño; Paul Broda

Publisher
Elsevier Science
Year
1994
Tongue
English
Weight
722 KB
Volume
253
Category
Article
ISSN
0008-6215

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✦ Synopsis

Phanerochaete chrysosporiwn is the best studied organism with respect to lignin degradation, but its degradation of the xylan component of lignocellulose is only now being studied . When grown on oat spelt xylan (mainly arabinoxylan), it produces an enzyme with (3-n-xylosidase and f-n-glucosidase activity. This enzyme was purified by ultrafiltration followed by ammonium sulphate precipitation, anion-exchange chromatography using DEAE Biogel and Mono Q, and gel filtration using Superose 12. It is extracellular, with an apparent Mr value of 44500 as determined by SDS-PAGE; the pI is 4 .67 and activity is maximal at pH 5 and 60°C . The enzyme is of particular interest because its principal activity is against laminaribiose (3-0-(3-D-glucopyranosyl-D-glucopyranose and laminarin [(1-> 3)-fl-D-glucan with ca. 3% of $41-> 6) branches] rather than cellobiose and xylobiose . It was competitively inhibited by D-glucono-1,5-lactone and deoxynojirimycin ; with p-nitrophenyl $-D-xylopyranoside as substrate, the K; values were 32 and 87 .5 µM, respectively, and with p-nitrophenyl p-D-glucopyranoside, they were 35 and 68 .7 µM, respectively. The Km values with p-nitrophenyl fl-D-xylopyranoside and p-nitrophenyl p-D-glucopyranoside as substrates were 3 .51 and 5 .30 mM, respectively.

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