Abstract:
PROBLEM TO BE SOLVED: To obtain a new alkali α-amylase having optimal condition or resistance to high alkali, having resistance to detergent component and useful as an additive component for detergents for dishes and detergents for clothes. SOLUTION: This alkali α-amylase is obtained by culturing Bacillus sp. KSM-SAA1112 (FERM P-15200), etc., which is an alkalophilic bacterium and has the following enzymatic properties: (1) capable of decomposing α-1,4 glucoside bond of starch, amylose, amylopectin and their partial decomposition product and not reacting with pullulan; (2) optimal pH 10-11 and acting in a range of pH 6.5 to 12.5 and extremely stable in a range of pH11.5; (3) 60 deg.C optimal temperature and capable of acting in a range of 20-70 deg.C; (4) 60,000±3,000 molecular weight; (5) about 4.1 isoelectric point; and (6) being hardly inhibited by surfactants.
Abstract:
PURPOSE: To obtain a gene for industrially mass-produce liquefied-type alkali α-amylase useful as an additive ingredient for detergent compositions for tableware and clothing. CONSTITUTION: This liquefied-type alkali α-amylase gene having a nucleotide sequence of the formula is obtained by breaking a chromosome DNA obtained from Bacillus sp. KSM-AP 1378 (FERM BP-3048) with a restriction enzyme such as Hind III followed by conducting PCR process. Plasmid pAML 100 is a recombinant plasmid composed of a 1.8kb fragment containing this gene and pUC18 4.4kb fragment, and a recombinant microbe containing the recombinant DNA molecule is pref. Escherichia coli HB 101 (pAML100) strain.
Abstract:
PURPOSE:To carry out the saccharification of a polysaccharide at a relatively low temperature under alkaline condition in high efficiency by treating a polysaccharide with an alkali pullulanase having amylase activity and produced by a bacterial strain belonging to genus Bacillus. CONSTITUTION:A polysaccharide is saccharified with alkali pullulanase Y having alpha-amylase activity and produced by a bacterial strain belonging to genus Bacillus. The polysaccharide is preferably starch, soluble starch, etc. The bacterial strain used in the present process is a bacillus having a cell size of (0.8-2.4)X(1.8-4.0)mum and bacteriological properties such as locomotivity and alkalophilic property, e.g. FERM 10886.
Abstract:
PURPOSE:To provide a cleanser composition effectively acting on the starch stains strongly adhered to table wares, fibers, etc., and having a remarkably improved cleanability by compounding an alkali pullulanase or alkali-resistant pullulanase having an alpha-amylase activity. CONSTITUTION:The objective composition comprises an alkali pullulanase or alkali-resistant pullulanase having an alpha-amylase activity in an amount of usually 0.1-10wt.%, the pullulanase being produced by Bacillus sp. KSM-AP1378 (FERM 10886). The purified enzyme may be used as the alkali or alkali-resistant pullulanase and a culture solution may be used as such as the crude enzyme.
Abstract:
PROBLEM TO BE SOLVED: To provide a new microorganism and a method for producing protein using the microorganism.SOLUTION: There is disclosed derepression of σD factor in a host microorganism in which a gene encoding a foreign protein is introduced by connecting under control of a σD factor-depending promoter.
Abstract:
PROBLEM TO BE SOLVED: To provide a polypeptide which has an excellent secretory property and to provide a recombinant microorganism.SOLUTION: The polypeptide is produced by joining (A) amino acid sequence to the N-terminus side in the amino acid sequence of a target protein or polypeptide other than the AmyE protein of Bacillus subtilis, and a recombinant microorganism is provided by introducing the base sequence encoding the amino acid sequence of the produced polypeptide to a host microorganism. The amino acid sequence is all or a consecutive part of the amino acid sequence shown in (A) sequence number 1, including at least the region of the first to 44th positions.
Abstract:
PROBLEM TO BE SOLVED: To provide a microorganism capable of controlling the expression gene-specifically.SOLUTION: A bacillus has: a target gene having a modified Shine-Dalgarno (SD) sequence; a plurality of rrn operons having a modified anti-SD sequence complementary to the modified SD sequence; and an rrn operon having an unmodified anti-SD sequence.
Abstract:
PROBLEM TO BE SOLVED: To provide a new gene expression method, a protein or polypeptide production method using the new gene expression method, and recombinant Bacillus subtilis used for the methods, especially, to provide a gene expression method and a protein or polypeptide production method using the gene expression method which are more efficient and simpler than the conventional methods, and to provide recombinant Bacillus subtilis used for the methods.SOLUTION: Bacillus subtilis is used as a host, and the recombinant Bacillus subtilis in which the amount of expression of the rocG gene in the genome is controlled according to culture phases is used. The method by which the amount of expressions of a target gene is efficiently controlled is provided.
Abstract:
PROBLEM TO BE SOLVED: To provide a variant of Bacillus subtilis from which a large region of genome is deleted based on a wild strain, and to provide a method for producing a gene product by using the variant. SOLUTION: The variant of the Bacillus subtilis has a genome structure obtained by deleting any one of the following regions in the genome of Bacillus subtilis 168 strain from the genome region of MGB874 strain of the variant of the Bacillus subtilis: (a) ybbU-ybfI region; (b) ydjM-cotA region; (c) yefA-yesX region; (d) yfiB-yfiX region; (e) yhcE-yhcU region; (f) yhaU-yhaL region; (g) yjbX-yjlB region; (h) xkdA-ykcC region; (i) bpr-ylmA region; (j) flgB-cheD region; (k) ynfF-ppsA region; (l) yoxC-yobO region; (m) spoVAF-spoIIAA region; (n) spoIIIAH-yqhV region; (o) ytvB-ytqB region; (p) yteA-ytaB region; (q) yuaJ-yugO region; (r) yusJ-mrgA region; (s) gerAA-yvrI region; (t) yvaM-yvbK region; (u) araE-yveK region; (v) yvdE-yvcP region; (w) gerBA-ywsC region; (x) ywrK-ywqM region; (y) spoIIID-ywoB region; (z) slp-ylaF region; (aa) licH-sigY region; (ab) yqeF-yrhK region; (ac) yuzE-yukJ region; and (ad) yncM-yndN region. COPYRIGHT: (C)2011,JPO&INPIT