Production, Purification, and Properties of a Pectin Lyase fromPseudomonas marginalisN6301
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منابع مشابه
Purification and Characterization of a Unique Pectin Lyase from Aspergillus giganteus Able to Release Unsaturated Monogalacturonate during Pectin Degradation
A pectin lyase, named PLIII, was purified to homogeneity from the culture filtrate of Aspergillus giganteus grown in submerged culture containing orange peel waste as carbon source. PLIII was able to digest apple pectin and citrus pectins with different degrees of methyl esterification. Interestingly, the PLIII activity was stimulated in the presence of some divalent cations including Pb(2+) an...
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Background: Alginate is a linear polysaccharide consisting of guluronate (polyG) and mannuronate (polyM) subunits. Methods: In the initial screening of alginate-degrading bacteria from soil, 10 isolates were able to grow on minimal medium containing alginate. The optimization of cell growth and alginate lyase (algL) production was carried out by the addition of 0.8% alginate and 0.2-0.3 M NaCl ...
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Isocitric lyase, or isocitritase, the enzyme which reversibly cleaves Lo (+)-isocitric acid to glyoxylic and succinic acids, has been identified in extracts of a number of microorganisms (l-6), and partially purified from Pseudomonas aeruginosa (7). Interest in this enzyme has been stimulated by its possible involvement in three important metabolic pathways: (a) glyoxylate formation from acetat...
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Isocitric lyase, or isocitritase, the enzyme which reversibly cleaves Lo (+)-isocitric acid to glyoxylic and succinic acids, has been identified in extracts of a number of microorganisms (l-6), and partially purified from Pseudomonas aeruginosa (7). Interest in this enzyme has been stimulated by its possible involvement in three important metabolic pathways: (a) glyoxylate formation from acetat...
متن کاملPurification and properties of N-acetylneuraminate lyase from Escherichia coli.
N-Acetylneuraminate lyase [N-acetylneuraminic acid aldolase EC 4.1.3.3] from Escherichia coli was purified by protamine sulfate treatment, fractionation with ammonium sulfate, column chromatography on DEAE-Sephacel, gel filtration on Ultrogel AcA 44, and preparative polyacrylamide gel electrophoresis. The purified enzyme preparation was homogeneous on analytical polyacrylamide gel electrophores...
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ژورنال
عنوان ژورنال: Bioscience, Biotechnology, and Biochemistry
سال: 1995
ISSN: 0916-8451,1347-6947
DOI: 10.1271/bbb.59.323