Purification and characterization of a pyruvated-mannose-specific xanthan lyase from heat-stable, salt-tolerant bacteria.

Abstract:

:A xanthanase complex secreted by a consortium of heat-stable, salt-tolerant bacteria includes a lyase that specifically removes terminal pyruvated beta-d-mannose residues from the side chains of xanthan gum. The enzyme was purified to homogeneity from the culture broth following ion-exchange chromatography and gel permeation chromatography. It consists of a single subunit of molecular weight 33,000. The enzyme is stable to 55 degrees C for more than 6 h in 20 mM sodium phosphate buffer (pH 5.0) containing 0.25 M NaCl. Optimal enzyme activity was observed at 0.05 M NaCl and a pH of 5. The enzyme has a pI of 3.7. It does not remove unsubstituted terminal beta-d-mannose residues from xanthan side chains nor does it hydrolyze p-nitrophenyl-beta-d-mannose. Treatment of xanthan with purified lyase results in a polysaccharide containing side chains terminating in an unsaturated 4,5-ene-glucuronic acid.

journal_name

Appl Environ Microbiol

authors

Ahlgren JA

doi

10.1128/AEM.57.9.2523-2528.1991

keywords:

subject

Has Abstract

pub_date

1991-09-01 00:00:00

pages

2523-8

issue

9

eissn

0099-2240

issn

1098-5336

journal_volume

57

pub_type

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