Molecular and enzymic properties of recombinant 1,2-α-mannosidase from Aspergillus saitoi overexpressed in Aspergillus oryzae cells

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Molecular and enzymic properties of recombinant 1, 2-alpha-mannosidase from Aspergillus saitoi overexpressed in Aspergillus oryzae cells.

For the construction of an overexpression system of the intracellular 1,2-alpha-mannosidase (EC 3.2.1.113) gene (msdS) from Aspergillus saitoi (now designated Aspergillus phoenicis), the N-terminal signal sequence of the gene was replaced with that of the aspergillopepsin I (EC 3.4.23.18) gene (apnS) signal, one of the same strains as described previously. Then the fused 1, 2-alpha-mannosidase ...

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Purification and properties of a beta-mannosidase from Aspergillus niger.

A beta-mannosidase (beta-D-mannoside mannohydrolase, EC 3.2.1.25) was purified to apparent homogeneity from the culture filtrate of the fungus, Aspergillus niger. The enzyme had an estimated molecular weight of about 120,000 and was a glycoprotein. Radioactive enzyme was prepared by growing the fungus in [14C]fructose, and this enzyme was used for the preparation of 14C-glycopeptides. The glyco...

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Cyclopiazonic Acid Biosynthesis of Aspergillus flavus and Aspergillus oryzae

Cyclopiazonic acid (CPA) is an indole-tetramic acid neurotoxin produced by some of the same strains of A. flavus that produce aflatoxins and by some Aspergillus oryzae strains. Despite its discovery 40 years ago, few reviews of its toxicity and biosynthesis have been reported. This review examines what is currently known about the toxicity of CPA to animals and humans, both by itself or in comb...

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Extracellular proteinases of Aspergillus oryzae.

Although the production of proteolytic enzymes by different strains of Aspergillus oryzae has been investigated in submerged culture (5, 15), in static liquid culture (3, 11), and on solid substratum (8-10), there appear to be few reports pertaining to the comparative evaluation of these different methods on the elaboration of proteinases by specific strains of A. oryzae. K. Mogi (13) compared ...

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Production and Characterization of a New α-Glucosidase Inhibitory Peptide from Aspergillus oryzae N159-1

An α-glucosidase inhibitor was developed from Aspergillus oryzae N159-1, which was screened from traditional fermented Korean foods. The intracellular concentration of the inhibitor reached its highest level when the fungus was cultured in tryptic soy broth medium at 27℃ for five days. The inhibitor was purified using a series of purification steps involving ultrafiltration, Sephadex G-25 gel p...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1999

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3390589