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- W1580263878 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." @default.
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- W1580263878 date "1991-09-01" @default.
- W1580263878 modified "2023-10-12" @default.
- W1580263878 title "Purification and Characterization of a Pyruvated-Mannose-Specific Xanthan Lyase from Heat-Stable, Salt-Tolerant Bacteria" @default.
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- W1580263878 doi "https://doi.org/10.1128/aem.57.9.2523-2528.1991" @default.
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