Publication:
Purification, characterization, and overexpression of thermophilic pectate lyase of bacillus sp. rn1 isolated from a hot spring in Thailand

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Issued Date

2009

Resource Type

Article

File Type

application/pdf

ISSN

9168451

DOI

10.1271/bbb.80287

Other identifier(s)

2-s2.0-65249146105

Rights Holder(s)

มหาวิทยาลัยศรีนครินทรวิโรฒ

Bibliographic Citation

Bioscience, Biotechnology and Biochemistry. Vol 73, No.2 (2009), p.268-273

Suggested Citation

Sukhumsiirchart W., Kawanishi S., Deesukon W., Chansiri K., Kawasaki H., Sakamoto T. Purification, characterization, and overexpression of thermophilic pectate lyase of bacillus sp. rn1 isolated from a hot spring in Thailand. Bioscience, Biotechnology and Biochemistry. Vol 73, No.2 (2009), p.268-273. doi:10.1271/bbb.80287 Retrieved from: https://hdl.handle.net/20.500.14740/7020

Title

Purification, characterization, and overexpression of thermophilic pectate lyase of bacillus sp. rn1 isolated from a hot spring in Thailand

Author(s)

Sukhumsiirchart W.
 Kawanishi S.
 Deesukon W.
 Chansiri K.
 Kawasaki H.
 Sakamoto T.

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.

Subject(s)

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

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URI

https://hdl.handle.net/20.500.14740/7020

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Scopus: Year 1983-2021

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