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Nucleotide sequence of the gene for an alkaline endoglucanase from an alkalophilic Bacillus and its expression in Escherichia coli and Bacillus subtilis.
The gene for an alkaline endoglucanase from the alkalophilic Bacillus sp. KSM-64 was cloned into the HindIII site of pBR322 and expressed in Escherichia coli HB101. The nucleotide sequence of a
A novel alkaline endoglucanase from an alkaliphilic Bacillus isolate: enzymatic properties, and nucleotide and deduced amino acid sequences
Abstract. A highly alkaline endo-1,4-β-glucanase (Egl) was purified to homogeneity from a culture broth of alkaliphilic Bacillus sp. strain KSM-N252. The optimal pH for activity was as high as 10,
Serum amyloid A, cytokines, and corticosterone responses in germfree and conventional mice after lipopolysaccharide injection.
The results suggest that the lower susceptibility to LPS and a smaller response to SAA elevation by LPS in germfree mice may result from less elevation in serum of these cytokines in these mice, which are known to mediate the acute phase response of SAA.
Application of the upstream region of a Bacillus endoglucanase gene to high-level expression of foreign genes in Bacillus subtilis.
A 0.4-kb ScaI-HpaI fragment, 199 bp upstream of the structural gene for alkaline endoglucanase, from the alkalophilic Bacillus sp. KSM-64, was found to be essential for the extracellular production
Construction, purification, and properties of a truncated alkaline endoglucanase from Bacillus sp. KSM-635.
Part of a 2.4-kb DNA fragment that encoded the amino-terminal 584 residues (65 kDa) of an alkaline endoglucanase from Bacillus sp. KSM-635 (941 amino acid residues; 105 kDa) was spontaneously deleted
Mutanase from a Paenibacillus isolate: nucleotide sequence of the gene and properties of recombinant enzymes.
The enzyme purified from the isolate appears to be truncated by proteolysis, and amongst several tested polysaccharides, the recombinant full-length enzyme specifically hydrolyzed mutan.
Nucleotide and amino-acid sequences of a new-type pectate lyase from an alkaliphilic strain of Bacillus.
Based on their amino-acid sequence homology, Pel-15E and PelA appear to belong to a new class of Pel family, although the enzymatic properties of both enzymes were quite different.
A new subtilisin family: nucleotide and deduced amino acid sequences of new high-molecular-mass alkaline proteases from Bacillus spp.
Six genes encoding high-molecular-mass subtilisins (HMSs) of alkaliphilic Bacillus spp. were cloned and sequenced. Their open reading frames of 2,394–2,424 bp encoded prosubtilisins of 798–808 amino
A stable isotope-aided NMR study of the active site of an endoglucanase from a strain of Bacillus.