Raw starch-digestive glucoamylase productivity of protease-less mutant from Aspergillus awamori var. kawachi.

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منابع مشابه

Expression and functional analysis of a hyperglycosylated glucoamylase in a parental host, Aspergillus awamori var. kawachi.

A modified glucoamylase gene (glaA) with an extra Thr- and Ser-rich Gp-I domain (T. Semimaru, M. Goto, K. Furukawa, and S. Hayashida, Appl. Environ. Microbiol. 61:2885-2890, 1995) was introduced into a mutant parental host, Aspergillus awamori var. kawachi, in which the original glaA gene had been completely deleted and replaced with the hygromycin phosphotransferase gene. The modified glaA was...

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Production and Characteristics of Raw-Starch-Digesting alpha-Amylase from a Protease-Negative Aspergillus ficum Mutant.

Mutational experiments were carried out to decrease the protease productivity of Aspergillus ficum IFO 4320 by using N-methyl-N'-nitro-N-nitrosoguanidine. A protease-negative mutant, M-33, exhibited higher alpha-amylaseactivity than the parent strain under submerged culture at 30 degrees C for 24 h. About 70% of the total alpha-amylase activity in the M-33 culture filtrate was adsorbed onto sta...

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Extraction and Purification of Glucoamylase and Protease Produced by Aspergillus awamori in a Single-Stage Fermentation

Simultaneous extraction and purification of glucoamylase and protease produced concomitantly by Aspergillus awamori Nakazawa MTCC 6652 in a single fermentor using solid-state fermentation (SSF) has been studied. Soaking for 2 h at room temperature (around 30 °C) in 10 % glycerol was found to be most suitable for optimum simultaneous extraction of glucoamylase and protease with the yield of 8645...

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Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution.

The three-dimensional structure of the pseudotetrasaccharide acarbose complexed with glucoamylase II(471) from Aspergillus awamori var. X100 has been determined to 2.4-A resolution. The model includes residues corresponding to 1-471 of glucoamylase I from Aspergillus niger, a single molecule of bound acarbose, and 535 sites for water molecules. The crystallographic R factor from refinement is 0...

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ژورنال

عنوان ژورنال: Agricultural and Biological Chemistry

سال: 1981

ISSN: 0002-1369,1881-1280

DOI: 10.1271/bbb1961.45.2675