Please use this identifier to cite or link to this item: http://ir.swu.ac.th/jspui/handle/123456789/15287
Title: Purification, characterization, and overexpression of thermophilic pectate lyase of bacillus sp. rn1 isolated from a hot spring in Thailand
Authors: Sukhumsiirchart W.
Kawanishi S.
Deesukon W.
Chansiri K.
Kawasaki H.
Sakamoto T.
Keywords: Bacillus sp
Bacillus spp
Cation exchanges
Culture filtrates
Electrospray-ionization mass spectrometries
Galacturonic acids
High temperatures
High-performance anion exchange chromatographies
Optimum pH
Overexpression
Pectate lyase
Polygalacturonic acids
Recombinant enzymes
Thailand
Thermophilic enzyme
Amines
Amino acids
Bacteriology
Calcium
Chromatographic analysis
Chromatography
Degradation
Electrospray ionization
Gene encoding
High performance liquid chromatography
Hot springs
Mass spectrometry
Organic acids
Polysaccharides
Purification
Enzymes
Bacillus sp.
pectate lyase
polysaccharide lyase
recombinant protein
amino acid sequence
article
Bacillus
chemistry
classification
enzymology
Escherichia coli
gene expression
genetics
isolation and purification
metabolism
microbiology
molecular genetics
nucleotide sequence
pH
phylogeny
temperature
Thailand
thermal spring
Amino Acid Sequence
Bacillus
Base Sequence
Escherichia coli
Gene Expression
Hot Springs
Hydrogen-Ion Concentration
Molecular Sequence Data
Phylogeny
Polysaccharide-Lyases
Recombinant Proteins
Temperature
Thailand
Issue Date: 2009
Abstract: A thermophilic pectate lyase, Pel SWU, was isolated from a culture filtrate of Bacillus sp. RN1 isolated from a hot spring in Ranong Province, Thailand. The enzyme was purified to homogeneity using cation-exchange and hydrophobic column chromatographies. The molecular mass of Pel SWU was estimated to be 33 kDa. The specific substrate was demethylated galacturonic acid. The enzyme was stable at pH 4.0-10.0 and at temperatures up to 70 -C in the presence of calcium and polygalacturonic acid (PGA). The optimum pH and temperature were 10.0 and 90 -C. The pel gene encoding Pel SWU was 1,023 bp, which corresponds to 341 amino acids. The properties of the recombinant enzyme was similar to those of Bacillus Pel SWU. Unsaturated di- and trigalacturonic acids were formed mainly as the final products of degradation by Pel SWU, as revealed by high-performance anion-exchange chromatography (HPAEC) and electrospray ionization mass spectrometry (ESI-MS) analyses. This thermophilic pectate lyase should be useful in the degradation of pectin networks at high temperature.
URI: https://www.scopus.com/inward/record.uri?eid=2-s2.0-65249146105&doi=10.1271%2fbbb.80287&partnerID=40&md5=6d041a8e4d022add242a95c0ec995f33
http://ir.swu.ac.th/jspui/handle/123456789/15287
ISSN: 9168451
Appears in Collections:SCOPUS 1983-2021

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