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1.  Draft Genome Sequence of Amphibacillus jilinensis Y1T, a Facultatively Anaerobic, Alkaliphilic and Halotolerant Bacterium 
Standards in Genomic Sciences  2013;8(3):491-499.
The genus Amphibacillus was established in 1990, and seven additional species were described in the past two decades. Amphibacillus jilinensis Y1T is a facultatively anaerobic and alkaliphilic bacterium isolated from a soda lake in China. Here we describe the structural and genetic features of the draft genome about the type strain Y1T (3,831,075 bp, with a G+C content of 37.27%). This is the first genome report of the Amphibacillus genus.
PMCID: PMC3910707  PMID: 24501633
Amphibacillus; facultative anaerobe; alkaliphilic bacterium; halotolerant; soda lake; two-component systems
2.  Complete Genome Sequence of Pelagibacterium halotolerans B2T 
Journal of Bacteriology  2012;194(1):197-198.
Pelagibacterium halotolerans B2T is a marine halotolerant bacterium that was isolated from a seawater sample collected from the East China Sea. Here, we present the complete genome sequence of the type strain P. halotolerans B2T, which consists of one chromosome (3,944,837 bp; 61.4% G+C content) and one plasmid (4,050 bp; 56.1% G+C content). This is the first complete genome of a member of the Pelagibacterium genus.
PMCID: PMC3256593  PMID: 22156395
3.  Cloning, Expression, and Characterization of a New β-Agarase from Vibrio sp. Strain CN41 ▿ †  
Applied and Environmental Microbiology  2011;77(19):7077-7079.
A new agarase, AgaACN41, cloned from Vibrio sp. strain CN41, consists of 990 amino acids, with only 49% amino acid sequence identity with known β-agarases. AgaACN41 belongs to the GH50 (glycoside hydrolase 50) family but yields neoagarotetraose as the end product. AgaACN41 was expressed and characterized.
PMCID: PMC3187099  PMID: 21821738
4.  Cloning and overexpression of a new chitosanase gene from Penicillium sp. D-1 
AMB Express  2012;2:13.
A chitosanase gene, csn, was cloned from Penicillium sp. D-1 by inverse PCR. The cDNA sequence analysis revealed that csn had no intron. The deduced CSN protein consists of 250 amino acids including a 20-amino acid signal peptide, and shared 83.6% identity with the family 75 chitosanase from Talaromyces stipitatus (B8M2R4). The mature protein was overexpressed in Escherichia coli and purified with the affinity chromatography of Ni2+-NTA. The novel recombinant chitosanase showed maximal catalytic activity at pH 4.0 and 48°C. Moreover, the activity of CSN was stable over a broad pH range of 3.0-8.0, and the enzymatic activity was significantly enhanced by Mg2+ and Mn2+. The CSN could effectively hydrolyze colloidal chitosan and chitosan, while could not hydrolyze chitin and carboxymethylcellulose (CMC). Due to the particular acidophily, CSN has the potential application in the recycling of chitosan wastes.
The GenBank/EMBL/DDBJ accession numbers for the 18S rRNA gene and chitosanase gene of strain D-1 are JF950269 and JF950270, respectively.
PMCID: PMC3308211  PMID: 22339878
Chitosanase; Penicillium sp.; Gene cloning; Expression
5.  Analysis of both chitinase and chitosanase produced by Sphingomonas sp. CJ-5*  
A novel chitinolytic and chitosanolytic bacterium, Sphingomonas sp. CJ-5, has been isolated and characterized. It secretes both chitinase and chitosanase into surrounding medium in response to chitin or chitosan induction. To characterize the enzymes, both chitinase and chitosanase were purified by ammonium sulfate precipitation, Sephadex G-200 gel filtration and DEAE-Sepharose Fast Flow. SDS-PAGE analysis demonstrated molecular masses of chitinase and chitosanase were 230 kDa and 45 kDa respectively. The optimum hydrolysis conditions for chitinase were about pH 7.0 and 36 °C, and these for chitosanase were pH 6.5 and 56 °C, respectively. Both enzymes were quite stable up to 45 °C for one hour at pH 5~8. These results show that CJ-5 may have potential for industrial application particularly in recycling of chitin wastes.
PMCID: PMC2064955  PMID: 17973345
Sphingomonas sp.; Chitinase; Chitosanase

Results 1-5 (5)