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Type: Journal article
Title: Barley arabinoxylan arabinofuranohydrolases: purification, characterization and determination of primary structures from cDNA clones
Author: Lee, R.
Burton, R.
Hrmova, M.
Fincher, G.
Citation: Biochemical Journal, 2001; 356(1):181-189
Publisher: Portland Press
Issue Date: 2001
ISSN: 0264-6021
Statement of
Robert C. Lee, Rachel A. Burton, Maria Hrmova and Geoffrey B. Fincher
Abstract: A family 51 arabinoxylan arabinofuranohydrolase, designated AXAH-I, has been purified from extracts of 7-day-old barley (Hordeum vulgare L.) seedlings by fractional precipitation with (NH(4))(2)SO(4) and ion-exchange chromatography. The enzyme has an apparent molecular mass of 65kDa and releases L-arabinose from cereal cell wall arabinoxylans with a pH optimum of 4.3, a catalytic rate constant (k(cat)) of 6.9s(-1) and a catalytic efficiency factor (k(cat)/K(m)) of 0.76 (ml x s(-1) x mg(-1)). Whereas the hydrolysis of a-L-arabinofuranosyl residues linked to C(O)3 of backbone (1 → 4)-beta-xylosyl residues proceeds at the fastest rate, alpha -L-arabinofuranosyl residues on doubly substituted xylosyl residues are also hydrolysed, at lower rates. A near full-length cDNA encoding barley AXAH-I indicates that the mature enzyme consists of 626 amino acid residues and has a calculated pI of 4.8. A second cDNA, which is 81% identical with that encoding AXAH-I, encodes another barley AXAH, which has been designated AXAH-II. The barley AXAHs are likely to have key roles in wall metabolism in cereals and other members of the Poaceae. Thus the enzymes could participate in the modification of the fine structure of arabinoxylan during wall deposition, maturation or expansion, or in wall turnover and the hydrolysis of arabinoxylans in germinated grain.
Keywords: Arabinofuranosidase; cell walls; enzymic hydrolysis; heteroxylans; wall metabolism
Rights: © 2001 Biochemical Society
RMID: 0020010114
DOI: 10.1042/bj3560181
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Appears in Collections:Agriculture, Food and Wine publications

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