In-vivo expression of chitinase-A from Serratia plymuthica UBCR_12

The chitinase-A [ChiA] encoding gene isolated from Serratia plymuthica UBCR_12 was cloned into E. coli DH5α using pGEM-T Easy vector and expressed in E. coli BL21 using pET-28a[+] vector. The length of the open reading frame [ORF] is 1692 bp composed of 563 amino acid residues precursor with a molec...

Full description

Saved in:
Bibliographic Details
Published in:IOP conference series. Earth and environmental science 2020-04, Vol.497 (1), p.12021
Main Authors: Fatiah, R, Syafriani, E, Tjong, D H, Suliansyah, I, Jamsari, J
Format: Article
Language:English
Subjects:
Amino acids
Bacteria
Chitin
Chitinase
Colloid chitin
E coli
Molecular weight
Open reading frames
Peptides
Protein structure
Serratia plymuthica
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The chitinase-A [ChiA] encoding gene isolated from Serratia plymuthica UBCR_12 was cloned into E. coli DH5α using pGEM-T Easy vector and expressed in E. coli BL21 using pET-28a[+] vector. The length of the open reading frame [ORF] is 1692 bp composed of 563 amino acid residues precursor with a molecular weight of 61 kDa. The protein structure composed of three domains: signal peptide, FnIII-like, and catalytic. The signal peptide domain was cleavages during transport through the periplasmic membrane, therefore the molecular weight of secreted ChiA is about 58 kDa. The recombinant ChiA Serratia plymuthica UBCR_12 that expressed in E. coli BL21 could hydrolyze colloidal chitin.
ISSN:1755-1307
1755-1315
DOI:10.1088/1755-1315/497/1/012021