Raw starch-digestive glucoamylase productivity of protease-less mutant from Aspergillus awamori var. kawachi.
نویسندگان
چکیده
منابع مشابه
Molecular Cloning of the Glucoamylase I Gene of AspergMus awamori var . kawachi for Localization of the Raw - starch - aMnity Site
متن کامل
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...
متن کاملProduction 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...
متن کاملExtraction 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...
متن کاملRefined 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