Purification and properties of inulin fructotransferase (depolymerizing) from Arthrobacter globiformis C11-1.
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منابع مشابه
Purification and Properties of Chitinase from Arthrobacter sp. NHB-10.
A chitinase was purified from the culture filtrate of nigeran-degrading Arthrobacter sp. NHB-10 by precipitation with ammonium sulfate and column chromatographies on DEAE-Sephadex A-50 and Superose 12. The final preparation was homogenous in polyacrylamide gel electrophoresis. The molecular weight of the purified enzyme was 30,000 and its isoelectric point was 6.8. The optimum pH and temperatur...
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A bacterial strain Arthrobacter globiformis A19 producing cyclic tetrasaccharide (CTS) was isolated from soil. The enzymes, 6-alpha-glucosyltransferase (6GT) and 3-alpha-isomaltosyltransferase (IMT), involved in the synthesis of CTS were purified to homogeneity. The molecular and enzymatic properties of IMT from A. globiformis were similar to those of enzymes from Bacillus globisporus C11 and N...
متن کاملIsolation and characterization of a bacteriophage of Arthrobacter globiformis.
A bacteriophage which reproduces on Arthrobacter globiformis ATCC 8010 was isolated from soil. This bacteriophage, designated phiAG8010, propagates either in soft agar or broth cultures of the host. Because of a slow adsorption rate, neither the latent period nor burst size was determined. The mature virion belongs to Bradley's group B and exhibits a hexagonal head measuring 69 nm (length) by 6...
متن کاملextraction and acetylation of purified trypsin from bovin pancreas and study of some its physico-chemical properties
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 اول2-Keto-D-gluconate-yielding membrane-bound D-glucose dehydrogenase from Arthrobacter globiformis C224: purification and characterization.
Glucose dehydrogenase (GlcDH) is the rate-limiting catalyst for microbial conversion of glucose to the important organic acid 2-ketogluconic acid (2KGlcA). In this study, a D-glucose dehydrogenase was purified from the industrial 2KGlcA producer Arthrobacter globiformis C224. After four purification steps, the GlcDH was successfully purified over 180 folds and specific activity of 88.1 U/mg. A ...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1988
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.52.291