Volume 18, Issue 1 (5-2023)
MGj 2023, 18(1): 85-95 |
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aghaei jeshvaghani Z, Hosseini R. Isolation, Molecular Cloning and Bioinformatics Evaluation of htrB Serine Protease Gene Extracted from Bacillus licheniformis. MGj 2023; 18 (1) : 8
URL: http://mg.genetics.ir/article-1-1638-en.html
URL: http://mg.genetics.ir/article-1-1638-en.html
Imam Khomeini International University
Abstract: (658 Views)
Proteases are the most important industrial enzymes. Microbial proteases, especially from Bacillus sp. are most widely exploited industrially. The aim of this study was isolation, cloning, sequencing and bioinformatics study of htrB protease serine gene extracted from Bacillus licheniformis. In this study, after extraction of bacterial DNA, one of the serine protease genes, htrB, was isolated from Bacillus licheniformis using the polymerase chain reaction technique. cloned into pTG19-T vector. DNA sequencing results confirmed the cloned segment. The cloned gene in the recombinant plasmid pTG19-htrB was cloned in pET41a (+). Based on nucleotide sequencing, the target gene has 1371 base pairs and encodes a protein with 456 amino acids. The calculated molecular weight and its predicted isoelectric point were 48.66 kDa and 4.85, respectively. Studies have shown that the enzyme is in the category of stable enzymes and will be expressed as a solution in Escherichia coli bacteria. The molecular structure, its biochemical and phylogenetic properties were investigated. Based on the results of phylogenetic studies, the obtained protein sequence showed high similarity to the sequences of other Bacillus species, such as B. subtilis, B. gobiensis and B. pumilus. The three-dimensional structure of the cloned enzyme was predicted using the PyMOL, I-TASSER, PHYRE2, RAPTORX and Modeller tools. After evaluating the drawn models, it was determined that the models provided by PHYRE2 and RAPTORX software are desirable models for predicting the three-dimensional structure of this protease.
Article number: 8
Type of Study: Applicable |
Subject:
Subject 04
Received: 2020/04/28 | Accepted: 2023/06/7 | Published: 2023/05/7
Received: 2020/04/28 | Accepted: 2023/06/7 | Published: 2023/05/7
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