Purification and properties of pectin lyase from Aspergillus japonicus.
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چکیده
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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In 1960 Albersheim, Neukom, and Deuel (1) reported on an enzyme present in a commercial pectic enzyme preparation (Pectin01 RlO, Rohm and Haas Company, Philadelphia) that degraded the a, 1 + 4-glycokidic bonds in pectin by a trans elimination of the proton on the 5th carbon atom of an anhydromethyl galacturonate unit with the oxygen of the adjacent glycosidic bond. Cleavage of the bonds in pect...
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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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آنزیم تریپسین در شرایط قلیایی ناپایدار می باشد .و فعالیت پروتئولیتیکی تریپسین منجربه خود هضمی آن در جایگاههای خاصی می گردد. بنابر این آنزیمی با ناپایداری بالا محسوب میگردد. در سالهای اخیر موفق شدند که با ایجاد تغیرات شیمیایی با اضافه کردن فلزات خاص ، کلسیم و یا عمل استیلاسیون منجر به افزایش پایداری آنزیم تریپسین گردند. مطالعات در حال حاضر نشان می دهد که تریپسین استیله شده فعالیت آنزیمی خود را ...
15 صفحه اولPurification and Zymography of lipase from Aspergillus niger PTCC5010
In this study, Aspergillus niger lipase after extraction of medium culture was precipitated with different percentages of acetone and purified by ion exchange chromatography using SP-sepharose HP and Q-sepharose HP. The process of purification of the anzyme was studied by electrophoresis and the molecular weight was detected and determined by Zymography using overlying containing phenol red and...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1975
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.39.313