2007Journal of Inner Mongolia University of TechnologyRequires access

CLONING AND SEQUENCING OF α-AMYLASE GENE FROM TWO WILD BACILLUS SUBTILIS STRAINS

Zhang Dong-yan

Open publisher page 0 citations

Abstract

0Two α-amylase-producing wild-type strains of Bacillus subtilis QSH4 and Bacillus subtilis SHX4 were screened from soil.The α-amylase genes from these strains were amplified via PCR technique using primers designed according to nucleotide sequence of α-amylase gene of Bacillus subtilis 168 strain.Sequence result showed that the genes from both strains were composed of 1948bp,and had an identity of 99.90%.They were shorter than α-amylase gene of 168 strain by 32bp(near the 3′ terminal) and had an identity of 96.97% with it.The predicted proteins for α-amylase genes of QSH4 and SHX4 strain were 477 amino acids long and 183 amino acids shorter than the α-amylase protein of 168 strain.As an inference from the result that the active site of the enzyme would be in three quarters of the N-terminal peptide.

About this research paper

What this paper is about

0Two α-amylase-producing wild-type strains of Bacillus subtilis QSH4 and Bacillus subtilis SHX4 were screened from soil.The α-amylase genes from these strains were amplified via PCR technique using primers designed according to nucleotide sequence of α-amylase gene of Bacillus subtilis 168 strain.Sequence result showed that the genes from both strains were composed of 1948bp,and had an identity of 99.90%.They were shorter than α-amylase gene of 168 strain by 32bp(near the 3′ terminal) and had an identity of 96.97% with it.The predicted proteins for α-amylase genes of QSH4 and SHX4 strain were 477 amino acids long and 183 amino acids shorter than the α-amylase protein of 168 strain.As an inference from the result that the active site of the enzyme would be in three quarters of the N-terminal peptide.

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

0Two α-amylase-producing wild-type strains of Bacillus subtilis QSH4 and Bacillus subtilis SHX4 were screened from soil.The α-amylase genes from these strains were amplified via PCR technique using primers designed according to nucleotide sequence of α-amylase gene of Bacillus subtilis 168 strain.Sequence result showed that the genes from both strains were composed of 1948bp,and had an identity of 99.90%.They were shorter than α-amylase gene of 168 strain by 32bp(near the 3′ terminal) and had an identity of 96.97% with it.The predicted proteins for α-amylase genes of QSH4 and SHX4 strain were 477 amino acids long and 183 amino acids shorter than the α-amylase protein of 168 strain.As an inference from the result that the active site of the enzyme would be in three quarters of the N-terminal peptide.

Key concepts: Bacillus subtilis, Amylase, Gene, Biology, Strain (injury), Nucleic acid sequence, Bacillaceae, Cloning (programming)

Related papers

Back to paper searchBrowse research topicsOriginal source
CLONING AND SEQUENCING OF α-AMYLASE GENE FROM TWO WILD BACILLUS SUBTILIS STRAINS — Research Paper | ScholarLens