Professors

Yaping Tian

By: Source: Date:2018-11-07 Updating:2018-11-07 View:


 

Professor

Tel:  0510-85918116

Email:  biochem@jiangnan.edu.cn

Web: 


Education & Experience

2006 – present            Professor, School of Biotechnology,   Jiangnan University

2010.4-2010.10         Research fellow, School of Life and Environmental Sciences, Tsukuba

 University

2001 – 2006              Ph.D of Fermentation   engineering,  Jiangnan University,

1999 – 2006              Associate   Professor, Wuxi   University of Light Industry

1995 – 1998              M.E.   of Fermentation engineering, Wuxi   University of Light Industry

1992 – 1999               Lecturer,   Wuxi University of Light   Industry


Research Fields

Tian's group focuses on the study   of active biomolecules (proteins, enzymes, polysaccharide, polypeptide,   etc.), including fermentation condition, extraction and purification,   characterization, structural and functional analysis, and their industrial applications.   Several main topics are listed below.

Prolyl   aminopeptidase   (PAP) is a type of exopeptidase which catalyzes the cleavage of N-terminal   proline residue from peptides and proteins specifically. Coupled with   endoprotease, PAP can improve the hydrolysis of proteins. Additionally, PAP   is widely used to remove the bitterness of hydrolysate, particularly   hydrolysate from proteins with high-content of proline. The heterogenous   expression of pap gene in safe strain B. subtilis can greatly   reduce the cost of industrial production of PAP. Prolyl aminopeptidase gene (pap) from Aspergillus   oryzae   was inserted into the plasmid pPIC9K and introduced into P. pastoris. Partially secretary   expression of PAP was achieved succesessfully. Further, The research included   the following aspects: the optimization of fermentation conditions,   purification of PAP by one-step, analysis of N-glycosylation, enzymatic   properties and the application of recombinant PAP on hydrolyzed glutenin.

Many   researches showed that EC found in alcoholic beverage and fermented foods   endangered human’s health. With the mechanism of EC formation in fermented   wines investigated, enzymatic elimination of EC is of great interest.   Thereforeacid   ureases   with good tolerance towards ethanol and acid attracted many researchers. The   recombinant urease apoprotein exhibited good stability in ethanol solution   and acidic conditions. Homologous modeling was used to predict the 3D   structure of α subunit of urease from P.rettgeri JN-B815. And the substrates   urea and urethane were docked with the predicted structure, respectively. The   docking results showed that three hydrogen bonds were formed between urea and amino acid residues in   the center of urease active site. The second structure prediction of urease was a little   different from refolded urease which was measured by circular dichroism   spectra. The refolded urease was consisted of 37.2% α   helix, 20.1% β sheet and 42.7% random coil.

Bioactive peptides derived from marine   protein resources through controlled   enzymolysis have broad application prospects in the fields of medicine, food,   feed, cosmetics and health care products. Tian's group   combines enzymatic reaction with membrane technology to construct a method   which can prepare laver antioxidative peptide, as well as comprehensively   utilize other fractionated active substances. In addition, the application of   LAP in the field of cosmetic was preliminary studied.

 

Selected Publications

1.        Kai-Dao   Wang,Ke-Hong Wang, Nandi Zhou,Yaping Tian*,Secretory   Expression, Purification, Characterization,and Application of an Aspergillus   oryzae Prolyl Aminopeptidase in Bacillus subtilis. Appl Biochem Biotechnol   2017,181:1611–1623.

2.        Xiao-Feng   Liu,Qian zhang,Nandi Zhou,Yaping Tian* Expression of an Acid Urease   with Urethanase Activity in E. coli and Analysis of Urease Gene. Mol   Biotechnol, 2017,59:84–97.

3.        Hongyu   Yang,Qiang Zhu,Nandi Zhou,Yaping Tian*,Optimized expression of prolyl   aminopeptidase in Pichia pastoris and its characteristics after   glycosylation. World J Microbiol Biotechnol, 2016,32:176-187.

4.        Qian   Zhang,Xiaohong Zha,Nandi Zhou,Yaping Tian* ,Preparation of crosslinked   enzyme aggregates (CLEAs) of acid urease with urethanase activity and their   application. J. Basic Microbiol., 2016, 56: 422-431.

5.        Hongxing   Xi, Yaping Tian*, Nandi Zhou, Zhemin Zhou and Wei She.   Characterization of An N-Glycosylated Bacillus Subtilis Leucine   Aminopeptidase Expressed in Pichia Pastoris J. Basic Microbiol. 2015,   55(2):236-246.

6.        Xiaoxia   Lu, Nandi Zhou, Yaping Tian*, Spectrophotometric determination of   ethyl carbamate through bi-enzymatic cascade reactions. Analytical Methods.   2015, 7(4): 1261-1264.

7.      Zhou N.D., Gu X.L., Zha X.H., Tian Y.P.*.,Purification   and Characterization of a Urethanase from Penicillium variabile, Appl Biochem   Biotechnol. 2014,172(1):351–360

8.      Wu, Y.T., Zhou, N.D., Zhou, Z.M.,Tian, Y.P*.,   et al.. A thermostable lysine aminopeptidase from Pseudomonas aeruginosa:   isolation, purification, characterization, and sequence analysis. J. Basic   Microbiol.2014,54, 1110-1119.

9.        Ding G.W., Zhou N.D., Tian Y.P.* Over-Expression of   a Proline Specific Aminopeptidase from Aspergillus oryzae JN-412 and Its   Application in Collagen Degradation. Appl Biochem. Biotechnol.,   2014,173(7):1765-1777.

 

 

 

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