路福平
个性化签名
- 姓名:路福平
- 目前身份:
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学术头衔:
博士生导师
- 职称:-
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学科领域:
微生物学
- 研究兴趣:
路福平,男,1967年5月出生,博士,教授,博士生导师,天津市“131人才”第一层次,天津科技大学生物工程学院院长。1996年毕业于华南理工大学并获得发酵工程专业博士学位。分别于2001年和2005年赴英国学习微生物分子生物学和英国高等教育管理体系。现任中国微生物学会理事、中国啤酒协会理事、中国微生物学会工业微生物专业委员会副主任委员、中国发酵协会酶制剂分会理事、天津市微生物学会副理事长、天津市专家协会会员。曾获首届天津市优秀青年人才奖、天津市优秀教师,2003年被授予“十五”立功先进个人,2006年获得天津市第八届青年科技奖,2007年获大学生挑战杯优秀指导教师奖。主持或完成的项目包括国家863计划、国家自然科学基金项目、国家科技基础条件平台项目、天津市科技攻关等科研项目。获得过省部级科技奖励一等奖1次,二等奖5次,三等奖1次。主编《微生物学》、《微生物学实验技术》、《工业微生物进展》、《发酵工程研究进展》,参编《现代英汉生物工程词典》、《生物制药工艺》、《乳酸菌及其发酵制品生产技术》和《工业微生物实验技术》等。近5年来发表论文180篇,SCI收录20篇。
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346
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成果数
7
【期刊论文】Adaptive response of Saccharomyces cerevisiae to hyperosmotic and oxidative stress
路福平, Fuping Lu a *, Yu Wang a, Dongqing Bai a, b, Lianxiang Du a
Process Biochemistry 40(2005)3614-3618,-0001,():
-1年11月30日
After being pretreated with a sublethal dose of either oxidative or hyperosmotic stress, Saccharomyces cerevisiae cells could withstand a subsequent higher dose of the same stress. Cross-adaptation also existed between the two stresses. Especially wild-type cells pretreated with 1%KCl (a hyperosmotic stress generating agent) and hyperosmotic-resistance mutant cells could significantly resist to lethal concentration of H2O2 (10mM). The addition of N-acetylcysteine (NAC) (30mg1-1) and MnSO4 (4mM) showed a strong reversion to hyperosmotic stress, which implicated that antioxidants participated in yeast adaptation to hyperosmosis. The two sublethal dose of stresses treatment, especially hyperosmosis, increased the level of GSH, CAT, SOD and total antioxidant capability (T-AOC) in yeast cells, which indicated adaptation between oxidative and hyperosmotic stresses was accompanied by the production of above several antioxidants. Furthermore, at least seven new proteins were induced by both oxidative and osmotic treatment.
Saccharomyces cerevisiae, Hyperosmotic stress, Oxidative stress, Protein oxidation, Adaptive response
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【期刊论文】Bioconversion of methyl-testosterone in a biphasic system
路福平, Bie Songtao *, Du lianxiang, Zhang Liming, Lu Fuping
Process Biochemistry 40(2005)3309-3313,-0001,():
-1年11月30日
The bioconversion of methyl-testosterone to methandienone in a biphasic system was studied using freeze-dried, thawed and growing Arthrobacter simplex AS 1.94* cells as biocatalyst. The biphasic system consists of an organic phase [30%(v/v)] with steroid 10g/L and an aqueous phase [70% (v/v)] containing the cells (5g.d.c.w/L). Carbon tetrachloride and Tween-80 were used as organic solvent and surfactant, respectively, and menadione was added as an external electron acceptor. The factors affecting the conversion rate in the two-phase system were investigated. The results showed that menadione was necessary in this system. Small amounts of product added to the reaction system can increase the dehydrogenation rate. Higher activities were obtained with thawed cells as compared to the freeze-dried and growing cells. Under the optimal operation conditions, more than 95% (w/w) of added methyl-testosterone could be converted to methandienone within 48h. Also, an easy way to recover the product in a high purity is proposed.
Methyl-testosterone, Methandienone, Bioconversion, Arthrobacter simplex, △1,, 2-Dehydrogenation, A biphasic system
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路福平, Zhongjun Chen, Heng Cai, Fuping Lu * & Lianxiang Du
Biotechnology Letters (2005) 27: 1745-1749,-0001,():
-1年11月30日
The expression of a synthetic gene encoding monellin, a sweet protein, in E. coli under the control of T7 promoter from phage is described. The single-chain monellin gene was designed based on the biased codons of E. coli so as to optimize its expression. Monellin was produced and accounted for 45% of total soluble proteins. It was purified to yield 43mg protein per gdry cell wt. The purity of the recombinant protein was confirmed by SDS-PAGE.
Escherichia col, expression, monellin, purification, sweet protein
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路福平, Cai Heng*, Zhongjun Chen, Lianxiang Du & Fuping Lu
Biotechnology Letters (2005) 27: 1731-1736,-0001,():
-1年11月30日
Alpha amylase gene from Bacillus licheniformis was mutated by site-directed mutagenesis to improve its acid stability. The mutant gene was expression in Bacillus subtilis under the control of the promoter of sacB gene which was followed by either the a-amylase leader peptide of Bacillus licheniformis or the signal peptide sequence of sacB gene of Bacillus subtilis. Both peptides efficiently directed the secretion of α-amylase from the recombinant B. subtilis cells. The extracellular a-amylase activities in two recombinants were 1001 and 2012Uml-1, respectively. The purity of the recombinant product was confirmed by SDSPAGE.
acid stability, α-amylase gene, Bacillus subtilis, expression
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【期刊论文】Purification and characterization of a novel fibrinolytic enzyme from Rhizopus chinensis 12
路福平, Liu Xiao-lan
Appl Microbiol Biotechnol (2005) 67: 209-214,-0001,():
-1年11月30日
A novel fibrinolytic enzyme from Rhizopus chinensis 12 was purified through ammonium sulfate precipitation, hydrophobic interaction, ionic exchange, and gel filtration chromatography. The purification protocol resulted in a 893-fold purification of the enzyme, with a final yield of 42.6%. The apparent molecular weight of the enzyme was 18.0 kDa, determined by sodium dodecylsulfate-polyacrylamide gel electrophoresis, and 16.6 kDa by gel filtration chromatography, which revealed a monomeric form of the enzyme. The isoelectric point of the enzyme estimated by isoelectric focusing electrophoresis was 8.5±0.1. The enzyme hydrolyzed fibrin. It cleaved the α, β, nd γ chains of fibrinogen simultaneously, and it also hydrolyzed casein and N-succinyl-Ala-Ala-Pro-PhepNA. The enzyme had an optimal temperature of 45℃, and an optimal pH of 10.5. EDTA, PCMB, and PMSF inhibited the activity of the enzyme, and SBTI, Lys, TPCK, and Aprotinine had no obvious inhibition, which suggested that the activity center of the enzyme had hydrosulfuryl and metal. The first 12 amino acids of the N-terminal sequence of the enzyme were S-V-S-E-I-Q-LM-H-N-L-G and had no homology with that of other fibrinolytic enzyme from other microbes.
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路福平, Haikuan Wang, Fuping Lu ∗, Yafan Sun & Lianxiang Du
Biotechnology Letters 26: 1569-1573, 2004.,-0001,():
-1年11月30日
The cDNA encoding for lignin peroxidase of Phanerochaete chrysosporium was expressed in the Pichia methanolica under the control of the alcohol oxidase (AUG1) promoterwhich was followed by either the lignin peroxidase leader peptide of Phanerochaete chrysosporium or the Saccharomyces cerevisiae α-factor signal peptide. Both peptides efficiently directed the secretion of lignin peroxidase from the recombinant yeast cell. The extracellular lignin peroxidase activity in two recombinants was 932U1−1 and 1933Ul−1. The purity of the recombinant product was confirmed by SDS-PAGE.
heterologous expression, lignin peroxidase, Phanerochaete chrysosporium, Pichia methanolica
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【期刊论文】枯草芽抱杆菌葡萄糖脱氢酶基因的克隆及在大肠杆菌中的高效表达
路福平, QIAO Jianjun, LU Fuping, CHEN Qiming, DU Lianxiang, GENG Yunqi
Acta Scientiarum Naturalium Universitatis Nankaiensis Vol. 37 No 2 Jun. 2004,-0001,():
-1年11月30日
利用PCR技术扩增得到来源于枯草芽孢杆菌的葡萄糖脱氢酶基因片段,并构建重组质粒pUC-T-GDH,然后将基因片段克隆于大肠杆菌表达载体pBV220中,得到表达质粒pBV-GDH。葡萄糖脱氢酶在含有表达质粒的基因工程菌株中得以诱导表达,聚丙烯酰胺凝胶电泳及薄层扫描结果表明,经诱导表达的葡萄糖脱氢酶约占基因工程菌株总蛋白的45%。葡萄糖脱氢酶活力测试表明,基因工程菌株无细胞抽提液中葡萄糖脱氢酶的活力为7.8U/毫克,约为对照组的30倍.实验结果初步说明,广泛应用于工业化生产的葡萄糖脱氢酶可以在基因工程菌株中得以大量表达并维持较高活力。
枯草芽孢杆菌, 基因表达, 葡萄糖脱氢酶, 聚丙烯酰胺凝胶电泳
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