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Appl Environ Microbiol. 1992 April; 58(4): 1082-1088
Copyright © 1992, American Society for Microbiology. All Rights Reserved.

Purification and Characterization of an {alpha}-L-Arabinofuranosidase from Butyrivibrio fibrisolvens GS113

Robert B. Hespell* and Patricia J. O'Bryan

Fermentation Biochemistry Research Unit, National Center for Agricultural Utilization Research, Agricultural Research Service, U.S. Department of Agriculture, 1815 N. University Street, Peoria, Illinois 61604

ABSTRACT

An {alpha}-L-arabinofuranosidase (EC 3.2.1.55) was purified from the cytoplasm of Butyrivibrio fibrisolvens GS113. The native enzyme had an apparent molecular mass of 240 kDa and was composed of eight polypeptide subunits of 31 kDa. The enzyme displayed an isoelectric point of 6.0, a pH optimum of 6.0 to 6.5, a pH stability of 4.0 to 8.0, and a temperature optimum of 45°C and was stable to 55°C. The Km and Vmax for p-nitrophenyl-{alpha}-L-arabinofuranoside were 0.7 mM and 109 µmol/min/mg of protein, respectively. The enzyme was specific for the furanoside configuration and also readily cleaved methylumbelliferyl-{alpha}-L-arabinofuranoside but had no activity on a variety of other nitrophenyl- or methylumbelliferyl glycosides. When the enzyme was incubated with cellulose, carboxymethyl cellulose, or arabinogalactan, no release of sugars was found. Arabinose was found as the hydrolysis product of oatspelt xylan, corn endosperm xylan, or beet arabinan. No activity was detected when either coumaric or ferulic acid ester linked to arabinoxylobiose was used as substrates, but arabinoxylobiose was degraded to arabinose and xylobiose. Since B. fibrisolvens GS113 possesses essentially no extracellular arabinofuranosidase activity, the major role of the purified enzyme is apparently in the assimilation of arabinose-containing xylooligosaccharides generated from xylosidase, phenolic esterase, xylanase, and other enzymatic activities on xylans.

FOOTNOTES

* Corresponding author.

Appl Environ Microbiol. 1992 April; 58(4): 1082-1088
Copyright © 1992, American Society for Microbiology. All Rights Reserved.



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Copyright © 1992 by the American Society for Microbiology. All rights reserved.