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Hydrolysis of wheat straw by a thermostable endoxylanase: Adsorption and kinetic studies by Caroline Zilliox; Philippe Debeire is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The adsorption of a purified 20.7 kDa thermostable endo-1-4-P-xylanase (EC 3.2.1.8) from a Bacillus sp. on wheat straw at 4°C was studied. Adsorption data fitted the Langmuir-type adsorption isotherm with the maximum amount of adsorbed xylanase being 521 kg protein g-' straw. Adsorption of the xylanase on straw, h&tin, and insoluble xylans was irreversible at 4°C. The extent of hydrolysis was quantified by the measurement of total neutral sugars liberatedfrom wheat straw-xylanase complexes at 60°C. Maximum hydrolysis was observed using 350 pg enzyme g-' straw and reached 11% of the xylans in the straw after 5 h of reaction. No proportionality could be found between the level of xylanase adsorption on straw and the extent of hydrolysis at 60°C. Adsorption and hydrolysis experiments indicated that all the bound xylanase was not hydrolytically active. This suggested that nonspec$c adsorption occurred on lignin. Analysis of the end products of the reaction indicated that xylose and neutral and uranic acid-containing xylo-oligosaccharides were the major compounds.

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Author

Caroline Zilliox; Philippe Debeire

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0141-0229)

Published

1998

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)