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Cao J.,Liaoning Entry Exit Inspection and Quarantine Bureau | Li J.,TaKaRa Biotechnology Dalian Co. | Zheng Q.,Liaoning Entry Exit Inspection and Quarantine Bureau | Xu J.,Liaoning Entry Exit Inspection and Quarantine Bureau
Food Science and Technology Research | Year: 2013

This study was to establish the optimal real-time PCR method for specific identification of puffer fish and monkfish. In this study, we designed the specific primers and probes for fish 12s and monkfish cytochrome oxidase subunit I (COI), and used them for specific identification of fish and monkfish. Our results showed that the specific primers and probes for monkfish COI could specifically identify 3 monkfish species, respectively, from total 42 samples of aquatic products. Moreover, the primers and probes for COI were very sensitive to detect 0.01% Lophius litulon content in the mixed sample of Theragra chalcogramma and Lophius litulon. Therefore, this method is simple, practical, sensitive and specific; is helpful and useful to identify the products of fish and monkfish. Source


Liu T.,Dalian Polytechnic University | Liu T.,Yanbian University | Yu H.,Dalian Polytechnic University | Zhang C.,Dalian Polytechnic University | And 13 more authors.
Applied and Environmental Microbiology | Year: 2012

A novel rutin-α-L-rhamnosidase hydrolyzing α-L-rhamnoside of rutin, naringin, and hesperidin was purified and characterized from Aspergillus niger DLFCC-90, and the gene encoding this enzyme, which is highly homologous to the α-amylase gene, was cloned and expressed in Pichia pastoris GS115. The novel enzyme was classified in glycoside-hydrolase (GH) family 13. © 2012, American Society for Microbiology. Source


Tan D.-H.,Dalian University of Technology | Tan D.-H.,Harbin Institute of Technology | Tan D.-H.,TaKaRa Biotechnology Dalian Co. | Qu Y.-Y.,Dalian University of Technology | And 3 more authors.
Harbin Gongye Daxue Xuebao/Journal of Harbin Institute of Technology | Year: 2010

To obtain novel salt-tolerant phenol-degrading bacteria and amplify the corresponding genes, a bacterium named W1 was isolated from the active sludge samples. 16S rRNA sequence analysis was used to identify the bacterium, and characteristics for phenol biodegradation were also studied. The 5'- and 3' -flanking regions of gene encoding the phenol hydroxylase were amplified from strain W1 by TAIL-PCR method. 1wt%-10wt% was showed that strain W1 was identified as Arthrobacter sp. The strain was capable of growing in the medium with 1wt%-10wt% NaCl and utilizing phenol as the sole carbon and energy source. And it could also degrade some other aromatic compounds such as p-methylphenol, salicylic acid and p-hydroquinone, etc. When concentration of NaCl was about 5wt%, 1000 mg · L-1 phenol could be degraded more than 90% by strain W1. The complete gene cluster was about 6 kb, of which the gene encoding the large subunit of phenol hydroxylase exhibited the highest similarity about 93% with the corresponding gene of Alcaligenes sp. Source


Liu T.,Yanbian University | Liu T.,Dalian Polytechnic University | Yu H.,Dalian Polytechnic University | Liu C.,Dalian Polytechnic University | And 7 more authors.
Applied Microbiology and Biotechnology | Year: 2013

A novel protodioscin-(steroidal saponin)-glycoside hydrolase, named protodioscin-glycosidase-1 (PGase-1), was purified and characterized from the Aspergillus oryzae strain. The molecular mass of this enzyme was determined to be about 55 kDa based on SDS-polyacrylamide gel electrophoresis. PGase-1 was able to hydrolyze the terminal 26-O-β-d-glucopyranoside of protodioscin (furostanoside) to produce dioscin (spirostanoside), and then further hydrolyze the terminal 3-O-(1 → 4)-α-l-rhamnopyranoside of dioscin to form progenin III. However, PGase-1 could hardly hydrolyze the 3-O-(1 → 2)-α-l-rhamnopyranoside of progenin III, 3-O-β-d-glucoside of trillin, and the 1-O-glycosides of ophiopogonin D (steroidal saponin). In addition, PGase-1 also could hydrolyze the α-d-galactopyranoside, β-d-glucopyranoside, and β-d-galactopyranoside of p-nitrophenyl- glycosides, but the enzyme could not hydrolyze the α-d-mannopyranoside, α-l-arabinopyranoside, α-d-glucopyranoside, β-d-xylopyranoside, and α-l-rhamnopyranoside of p-nitrophenyl-glycosides. These new properties of PGase-1 were significantly different from those of previously described steroidal saponin-glycosidases and the glycosidases currently described in Enzyme Nomenclature by the NC-IUBMB. The gene (termed as pgase-1) encoding PGase-1 was cloned, sequenced, and expressed in Pichia pastoris GS115. The complete nucleotide sequence of pgase-1 consists of 1,725 bp. The recombinant PGase-1 from recombinant P. pastoris GS115 strain also showed the activity hydrolyzing glycosides of steroidal saponins which was similar to that of the wild-type PGase-1 from A. oryzae. The PGase-1 gene is highly similar to Aspergilli α-amylase (EC 3.2.1.1), and PGase-1 should be classified as glycoside hydrolase family 13 by the method of gene sequence-based classification. But the enzyme properties of PGase-1 are different from those of α-amylase in this family. © 2013 Springer-Verlag Berlin Heidelberg. Source

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