肖亚中
从事学科专业为生化与分子生物学,主要研究兴趣:基因表达调控的分子机制;生物催化原理及应用;微生物通讯机制。研究领域包括基因工程,酶与酶工程,环境和工业生物技术等。
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- 姓名:肖亚中
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学术头衔:
博士生导师
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学科领域:
生物化学
- 研究兴趣:从事学科专业为生化与分子生物学,主要研究兴趣:基因表达调控的分子机制;生物催化原理及应用;微生物通讯机制。研究领域包括基因工程,酶与酶工程,环境和工业生物技术等。
肖亚中,博士(后),教授,博士生导师,安徽大学学位与学科建设办公室主任。
1984年本科毕业于安徽大学生物系生化微生物专业,获学士学位。1994年在中国科技大学获硕士学位。1997-1998年在 Hong Kong University of Science & Technology生化系任访问学者。2002年毕业于中国科技大学生化与分子生物学专业,获博士学位。2005-2006年在美国Florida International University做博士后研究。
1984年以来在安徽大学生物系和生命科学学院从事教学和科研工作。历任助教、讲师、副教授、教授,微生物教研室主任、生命学院副院长、校学位与学科建设办副主任和校研究生院(筹)副院长等。现任安徽大学学术委员会委员,安徽大学学位委员会委员,兼任中国微生物学会常务理事,中国微生物学会基础微生物专业委员会副主任委员,安徽省微生物学会理事长(法人),安徽省生化与分子生物学会副理事长,安徽省生物工程学会副理事长,《生物工程学报》编委,《微生物学通报》常务编委和《生物学杂志》副主编等。先后被遴选为安徽省高校中青年骨干教师培养对象(1995)和学科带头人培养对象(2003)、安徽大学中青年骨干教师(1996)、安徽大学学术创新团队计划项目负责人(2005)、安徽省学术与技术带头人后备人选(2005)、中科院合肥物质研究院博士生导师(2007)和安徽省学术与技术带头人(2008)。是安徽大学教书育人先进个人(1991)、安徽大学优秀教师(1995)、安徽省首届陈香梅教育奖(1996)、安徽大学青年教师教学优秀奖一等奖(2001)和“挑战杯”大学生课外学术科技作品竞赛指导奖(2004)等获得者,是安徽省首届优秀硕士学位论文指导老师(2008)。
从事学科专业为生化与分子生物学,主要研究兴趣:基因表达调控的分子机制;生物催化原理及应用;微生物通讯机制。研究领域包括基因工程,酶与酶工程,环境和工业生物技术等。主持国家高技术发展计划(863)项目子课题、国家自然科学基金、教育部科学技术研究重点项目、安徽省科技攻关重点和安徽省优秀青年科技基金等研究课题20项。在国内外学术期刊发表研究论文68篇,其中被SCI收录22篇,EI收录9篇。主译出版学术专著1部,申报国家发明专利6项,获授权专利3项。获得安徽省科技进步奖1项(排名第一),安徽省高等学校优秀科技成果奖1项(排名第一),安徽省教学成果奖1项(排名第二),安徽省自然科学优秀学术论文一等奖1项(排名第一)。
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【期刊论文】Gongronella sp. induces overproduction of laccase in Panus rudis
肖亚中, Fen Wei*, Yuzhi Hong*, Juanjuan Liu, Jing Yuan, Wei Fang, Hui Peng and Yazhong Xiao
Journal of Basic Microbiology 2010, 50, 98-103,-0001,():
-1年11月30日
Laccase is usually produced via chemical induction and is also synthesized by hosts in interaction with the typical bio-control genus Trichoderma. In this study, we found that a newly isolated non-laccase-producing fungus, Gongronella sp. W5, could induce overproduction of laccase in Panus rudis. The enzyme activity, 148,200 U l-1, was 25 times higher than the activity obtained from a chemical induction using copperlo-toluidine as inducers. A new laccase isozyme from the interaction of P. rudis and G. W5 was purified and characterized. A further test showed that some pH resistant metabolites secreted by G. W5 acted as signals to induce P. rudis laccase. Laccase is also highly expressed by Trametes sp. AH28-2 in interaction with Trichoderma sp. ZH1. However, no laccase activity was observed from the cross-over interactions of P. rudis-Trichoderma sp. ZH1 or Trametes sp. AH28-2-G.W5.
Gongronella/, Laccase/, Microbial interaction/, Panus rudis/, Trichoderma
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【期刊论文】Preparation and Application of Polyclonal Antibody against a Recombinant Laccase
肖亚中, Yinghai Xu, Yuzhi Hong, Yazhong Xiao, and Wei Fang
Cellular & Molecular Immunology Volume 4 Number 4 August 2007,-0001,():
-1年11月30日
A laccase gene from Trametes sp. 420 was recombinantly expressed in Pichia pastoris, producing the enzyme rLacD. Six mutant enzymes were produced by site-directed mutation at six potential glycosylation sites in the enzyme rLacD respectively. To probe the mutants with lower activities sensitively and specifically, the antiserum containing specific polyclonal antibodies were prepared by immunizing healthy male rabbits, about 4-month-old and 2 kilogram weight, using pure rLacD as an immunogen. Antibodies were collected after the fifth immunization injection. The antiserum had titres of 1:32 in double immunodiffusion test and of 1:128,000 in enzyme-linked immunosorbent assay (ELISA). The results obtained by Western blot analysis showed that the antiserum could react with rLacD and its mutants with highly specific and sensitive affinities.antiserum, laccase, polyclonal antibody
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肖亚中, Yuzhi Hong, Yazhong Xiao, Hongmin Zhou, Wei Fang, Min Zhang, Jun Wang, Lijun Wu & Zengliang Yu
FEMS Microbiol Lett 258(2006)96-101,-0001,():
-1年11月30日
A laccase cDNA from Trametes sp. AH28-2 was expressed in Pichia pastoris, with the highest expression level of 4.0 mg L-1 (1360Umg-1). The apparent Km (24.6mM) for ABTS (2,20-azinobis [3-ethylbenzothia-zoline-6-sulfonic acid]) and the carbohydrate content of the recombinant laccase A (rLacA) are approximately identical to those of the native LacA (nLacA). However, the two enzymes differed in the pH optimum when both ABTS and guaiacol served as substrates. The optimum pH for enzyme stability is 5.5 for rLacA. Thermal stability was also investigated. The mutagenesis of rLacA utilizing low-energy nitrogen ion implantation resulted in the isolation of a yeast clone that produced 7.7 mg L- 1(1085Umg 1) of laccase, 92.5% more than the nonirradiated control (4.0 mg L-1). Compared with rLacA, the mutant LacA (mLacA) with five amino-acid residue changes in the coding sequence showed a slight change in its catalytic ability but superior thermal stability.
Trametes, laccase, Pichia pastoris, recombinant expression, low-energy nitrogen ion implantation.,
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【期刊论文】Degradation of lignin in pulp mill wastewaters by white-rot fungi on biofilm
肖亚中, Juan Wu a, b, Ya-Zhong Xiao b, Han-Qing Yu a, *
Bioresource Technology 96(2005)1357-1363,-0001,():
-1年11月30日
An investigation was conducted to explore the lignin-degrading capacity of attached-growth white-rot fungi. Five white-rot fungi, Phanerochaete chrysosporium, Pleurotus ostreatus, Lentinus edodes, Trametes versicolor and S22, grown on a porous plastic media, were individually used to treat black liquor from a pulp and paper mill. Over 71% of lignin and 48% of chemical oxygen demand (COD) were removed from the wastewater. Several factors, including pH, concentrations of carbon, nitrogen and trace elements in wastewater, all had significant effects on the degradation of lignin and the removal of COD. Three white-rot fungi, P. chrysosporium, P. ostreatus and S22, showed high capacity for lignin degradation at pH 9.0-11.0. The addition of 1 g l-1 glucose and 0.2 g l-1 ammonium tartrate was beneficial for the degradation of lignin by the white-rot fungi studied.
Black liquor, Biodegradation, Lignin, COD, White-rot fungi
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肖亚中, Y. Z. Xiao, Q. Chen, J. Hang, Y. Y. Shi, Y. Z. Xiao, J. Wu, Y. Z. Hong, Y. P. Wang
Mycologia, 96(1), 2004, pp. 26-35.,-0001,():
-1年11月30日
The white-rot fungus Trametes sp. AH28-2 can synthesize extracellular laccase by induction in cellobiose-based liquid culture medium. Both yields and composition of laccase isozymes, produced by Trametes sp. AH28-2, would be quite different with induction by different small-molecule aromatic compounds, o-toluidine, guaiacol and 3,5-dihydroxytoluene, which affected microbial growth and the synthesis of laccase isozymes differentially. Higher concentrations of the three inducers could considerably increase laccase isozymes yields but not change the laccase composition. Coculturing of Trametes sp. AH28-2 with either Aspergillus oryzae or Gloeophyllum trabeum showed a few effects on laccase production. Laccase isozyme, laccase B, was selectively induced by 3,5-dihydroxytoluene and purified to homogeneity by two-step chromatography. Purified laccase B appeared as blue, with a broad peak at about 600 nm and a shoulder peak at about 330 nm. The ratio of absorbance at 280 nm to that at 600 nm was 21. Every molecule of laccase B had approximately four copper atoms. Molecular mass of laccase B was estimated to be 74 kDa on SDS-PAGE, 72 kDa by FPLC and was determined to be 71 454 Da by mass spectrum. After being treated with N-glycosidase F, laccase B lost 25% of its molecular mass. The isoelectric point of laccase B was 4.0. Its optimal pH and temperature for oxidizing guaiacol were respectively 4.7 and 45 C. The half-life of the enzyme at 60 C was 14.0 min. The Accepted for publication May 31, 2003. 1 Corresponding author. E-mail: yyshi@ustc.edu.cn enzyme showed a good stability in a range of pH value of 3.5-7.5. The Km values of the enzyme toward substrates syringaldazine, guaiacol, ABTS, and DMOP were respectively 28.0, 1249.0, 177.0 and 109.8 mM. The corresponding Vmax are 504.0, 1910.0, 117.4 and 159.0 mM min21 mg21. In addition, activity of laccase B was inhibited strongly by sodium azide and cyanide, mildly by SDS and trifluoroacetic acid, but only weakly by dimethyl sulfoxide.
Aromatic compounds,, 3,, 5-dihydroxytoluene,, guaiacol,, laccase isozyme,, o-toluidine,, Trametes sp., AH28-2
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