Please use this identifier to cite or link to this item: http://ir.swu.ac.th/jspui/handle/123456789/14489
Title: Characterization of thermophilic halotolerant Aeribacillus pallidus TD1 from tao dam hot spring, Thailand
Authors: Yasawong M.
Areekit S.
Pakpitchareon A.
Santiwatanakul S.
Chansiri K.
Keywords: fatty acid
pectate lyase
fatty acid
RNA 16S
Aeribacillus pallidus
article
bacterial cell
bacterial growth
bacterial strain
bacterium examination
bacterium identification
bacterium isolation
cell motility
cell structure
controlled study
DNA sequence
enzyme activity
image analysis
nonhuman
nucleotide sequence
photometry
sequence analysis
Thailand
thermal spring
thermophilic bacterium
Bacillaceae
classification
DNA base composition
genetics
isolation and purification
metabolism
microbiology
physiology
ultrastructure
Bacteria (microorganisms)
Posibacteria
Bacillaceae
Base Composition
Fatty Acids
Hot Springs
RNA, Ribosomal, 16S
Thailand
Issue Date: 2011
Abstract: The bacterial strain TD1 was isolated from Tao Dam hot spring in Thailand. Strain TD1 was Gram positive, rod-shaped, aerobic, motile, and endospore forming. The cell was 2.0-40 μm in length and about 0.4 μm in diameter. The optimum growth occurred at 55-60 °C and at pH 7-8. Strain TD1 was able to grow on medium containing up to 10% NaCl. The DNA G+C content was 38.9 mol%. The cellular fatty acid content was mainly C16:0, which comprised 25.04% of the total amount of cellular fatty acid. 16S rDNA showed 99% identity to Aeribacillus pallidus DSM 3670 T. Bayesian tree analysis strongly supported the idea that strain TD1 is affiliated with genus Aeribacillus, as Aeribacillus pallidus strain TD1. Although the 16S rDNA of A. pallidus strain TD1 is similar to that of A. pallidus DSM 3670 T, some physiological properties and the cellular fatty acid profiles differ significantly. A. pallidus strain TD1 can produce extracellular pectate lyase, which has not been reported elsewhere for other bacterial strains in the genus Aeribacillus. A. pallidus strain TD1 may be a good candidate as a pectate lyase producer, which may have useful industrial applications. © 2011 by the authors; licensee MDPI, Basel, Switzerland.
URI: https://www.scopus.com/inward/record.uri?eid=2-s2.0-80052185258&doi=10.3390%2fijms12085294&partnerID=40&md5=281bd48bda5961b09ac004c02afc0f34
http://ir.swu.ac.th/jspui/handle/123456789/14489
ISSN: 14220067
Appears in Collections:SCOPUS 1983-2021

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