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Ahlgren JA. Purification and characterization of a pyruvated-mannose-specific xanthan lyase from heat-stable, salt-tolerant bacteria. Appl Environ Microbiol. 1991;57(9):2523-8doi: 10.1128/aem.57.9.2523-2528.1991.
Ahlgren, J. A. (1991). Purification and characterization of a pyruvated-mannose-specific xanthan lyase from heat-stable, salt-tolerant bacteria. Applied and environmental microbiology, 57(9), 2523-8. https://doi.org/10.1128/aem.57.9.2523-2528.1991
Ahlgren, J A. "Purification and characterization of a pyruvated-mannose-specific xanthan lyase from heat-stable, salt-tolerant bacteria." Applied and environmental microbiology vol. 57,9 (1991): 2523-8. doi: https://doi.org/10.1128/aem.57.9.2523-2528.1991
Ahlgren JA. Purification and characterization of a pyruvated-mannose-specific xanthan lyase from heat-stable, salt-tolerant bacteria. Appl Environ Microbiol. 1991 Sep;57(9):2523-8. doi: 10.1128/aem.57.9.2523-2528.1991. PMID: 16348550; PMCID: PMC183613.
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Appl Environ Microbiol. 1991 Sep;57(9):2523-8. doi: 10.1128/aem.57.9.2523-2528.1991.

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

Applied and environmental microbiology

J A Ahlgren

Affiliations

  1. Biopolymer Research Unit, National Center for Agricultural Utilization Research, Agricultural Research Service, U.S. Department of Agriculture, 1815 North University Street, Peoria, Illinois 61604.

PMID: 16348550 PMCID: PMC183613 DOI: 10.1128/aem.57.9.2523-2528.1991

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.

References

  1. Nature. 1970 Aug 15;227(5259):680-5 - PubMed
  2. J Biol Chem. 1959 Apr;234(4):705-9 - PubMed
  3. Appl Environ Microbiol. 1986 Jul;52(1):37-44 - PubMed
  4. Carbohydr Res. 1975 Dec;45:275-82 - PubMed
  5. J Gen Microbiol. 1987 Nov;133(11):3129-34 - PubMed
  6. Chem Ind. 1970 Jun 6;23:747-8 - PubMed
  7. Anal Biochem. 1983 Mar;129(2):277-87 - PubMed
  8. J Biochem. 1964 Feb;55:205-8 - PubMed
  9. Appl Environ Microbiol. 1982 Jul;44(1):5-11 - PubMed

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