Purification and characterization of two alpha-L-arabinofuranosidases from Streptomyces diastaticus.

Abstract:

:A nonsporulating strain of Streptomyces diastaticus producing alpha-L-arabinofuranosidase activity (EC 3.2-1.55) was isolated from soil. Two alpha-L-arabinosidases were purified by ion-exchange chromatography and chromatofocusing. The enzymes had molecular weights of 38,000 (C1) and 60,000 (C2) and pIs of 8.8 and 8.3, respectively. The optimum pH range of activity for both enzymes was between 4 and 7. The apparent Km values with p-nitrophenyl arabinofuranoside as the substrate were 10 mM (C1) and 12.5 mM (C2). C1 retained 50% of its activity after 8 h of incubation at 25 degrees C, while C2 retained 80% activity. After 3 h of incubation at 50 degrees C, C1 lost 90% of its initial activity while C2 lost only 40%. The purified enzymes hydrolyzed p-nitrophenyl alpha-L-arabinofuranoside and liberated arabinose from arabinoxylan and from a debranched beta-1,5-arabinan.

journal_name

Appl Environ Microbiol

authors

Tajana E,Fiechter A,Zimmermann W

doi

10.1128/AEM.58.5.1447-1450.1992

keywords:

subject

Has Abstract

pub_date

1992-05-01 00:00:00

pages

1447-50

issue

5

eissn

0099-2240

issn

1098-5336

journal_volume

58

pub_type

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