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Purification and Characterization of a Pyruvated-Mannose-Specific Xanthan Lyase from Heat-Stable, Salt-Tolerant Bacteria

By Jeffrey A. Ahlgren

Abstract

A xanthanase complex secreted by a consortium of heat-stable, salt-tolerant bacteria includes a lyase that specifically removes terminal pyruvated β-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°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 β-d-mannose residues from xanthan side chains nor does it hydrolyze p-nitrophenyl-β-d-mannose. Treatment of xanthan with purified lyase results in a polysaccharide containing side chains terminating in an unsaturated 4,5-ene-glucuronic acid

Topics: Enzymology and Protein Engineering
Year: 1991
OAI identifier: oai:pubmedcentral.nih.gov:183613
Provided by: PubMed Central
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