Publications by authors named "Yigang Teng"
Unlabelled: Hepatocellular carcinoma (HCC) is one of the most common cancers and the third leading cause of death from cancer worldwide. HCC has a very poor prognosis because of tumor invasiveness, frequent intrahepatic spread, and extrahepatic metastasis. The molecular mechanism of HCC invasiveness and metastasis is poorly understood.
View Article and Find Full Text PDFThe endoglucanase, EGA, from Bacillus sp. AC-1 comprises a glycosyl hydrolase family-9 catalytic module (CM9) and a family-3 carbohydrate-binding module (CBM3). Seven aromatic residues were subjected to site-directed mutagenesis in both CBM3 and EGA to investigate their roles in enzyme thermostability.
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- Three endoglucanase cDNAs (eg65a, eg65b, eg65c) were cloned from the mollusk Ampullaria crossean to study their functions.
- These enzymes and their respective catalytic and carbohydrate-binding modules were expressed in different systems (Pichia pastoris and E. coli) for analysis.
- The binding assays showed that EG65b-CBM and EG65c-CBM effectively bound to certain polysaccharides, while EG65a-CBM did not, marking the first characterization of animal cellulase CBMs.
Purification and characterization of a novel endo-β-1,4-glucanases , AfEG22, from the giant snail, Achatina fulica frussac.
Acta Biochim Biophys Sin (Shanghai)
October 2010
Article Synopsis
- At least three endo-β-1,4-glucanases were confirmed in the digestive juice of the giant snail, Achatina fulica, using a Congo red staining assay.
- A novel enzyme, AfEG22, was purified and showed a carboxymethyl cellulose hydrolytic activity of 12.3 U/mg protein and had a molecular mass of 22,081 Da.
- AfEG22 exhibited high stability and optimal activity at pH 4.0 and 50°C, marking it as the first reported endo-β-1,4-glucanase with such characteristics from A. fulica.
Identification, expression, and characterization of the highly conserved D-xylose isomerase in animals.
Acta Biochim Biophys Sin (Shanghai)
February 2009
D-xylose is a necessary sugar for animals. The xylanase from a mollusk, Ampullaria crossean, was previously reported by our laboratory. This xylanase can degrade the xylan into D-xylose.
View Article and Find Full Text PDFThe N-terminal cellulose-binding domain of EGXA increases thermal stability of xylanase and changes its specific activities on different substrates.
Acta Biochim Biophys Sin (Shanghai)
November 2008
A full-length EGXA enzyme from a mollusk, Ampullaria crossean, was cloned into pFastBac vector and then heterogeneously expressed in insect Tn5 cells. Its natural N-terminal signal peptide worked well in the insect Tn5 cells. The recombinant EGXA was a 63 kDa protein and had active endo-beta-1,4-glucanase (EC 3.
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