Article Per Year (5 Year)
p-Index From 2021 - 2026
0
P-Index
This Author published in this journals
All Journal HAYATI Journal of Biosciences
LINDA SUKMARINI
Carbohydrate and Bioengineering Research Group, Research Center for Biotechnology, Indonesian Institute of Sciences
Agriculture, Biological Sciences & Forestry Earth & Planetary Sciences

Published : 1 Documents Claim Missing Document
Claim Missing Document
Check
Articles

Found 1 Documents
Search

 1 
A xylanase gene, xynA, has been cloned from thermophilic strain Geobacillus stearothermophilus, which was isolated from marine Tanjung Api, Indonesia. The polymerase chain reaction product of 1266 bp of xynA gene consisted of 1221 bp open reading frame and encoded 407 amino acids including 30 residues of signal peptide. The sequence exhibited highest identity of 98.7% in the level of amino acid, with an extracellular endo-1,4-β-xylanase from G. stearothermophilus T-6 (E-GSX T-6) of the glycoside BUDI SAKSONO; LINDA SUKMARINI
HAYATI Journal of Biosciences Vol. 17 No. 4 (2010): December 2010
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.17.4.189

Abstract

A xylanase gene, xynA, has been cloned from thermophilic strain Geobacillus stearothermophilus, which was isolated from marine Tanjung Api, Indonesia. The polymerase chain reaction product of 1266 bp of xynA gene consisted of 1221 bp open reading frame and encoded 407 amino acids including 30 residues of signal peptide. The sequence exhibited highest identity of 98.7% in the level of amino acid, with an extracellular endo-1,4-β-xylanase from G. stearothermophilus T-6 (E-GSX T-6) of the glycoside hydrolase family 10 (GH10). A comparative study between the local strain G. stearothermophilus (GSX L) and E-GSX T-6 on homology of amino acid sequence indicated five differents amino acids in the gene. They were Threonine/Alanine (T/A), Asparagine/Aspartate (N/D), Lysine/Asparagine (K/N), Isoleucine/Methionine (I/M), Serine/Threonine (S/T) at the position 220, 227, 228, 233, and 245, respectively. Protein structural analysis of those differences suggested that those amino acids may play role in biochemical properties such as enzyme stability, in particular its thermostability.
Co-Authors BUDI SAKSONO