曲音波
纤维素酶和可再生资源微生物转化技术。
个性化签名
- 姓名:曲音波
- 目前身份:
- 担任导师情况:
- 学位:
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学术头衔:
博士生导师, 教育部“新世纪优秀人才支持计划”入选者
- 职称:-
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学科领域:
微生物学
- 研究兴趣:纤维素酶和可再生资源微生物转化技术。
曲音波,山东大学教授、博士、博士生导师。现任山东大学生物科学学院院长,微生物技术国家重点实验室主任。中国微生物学会常务理事、基础微生物学专业委员会主任;中国生物工程学会工业和环境生物技术专业委员会副主任;山东微生物学会副理事长。主要研究领域 资源环境微生物技术,微生物酶化学。主要研究方向:纤维素酶和可再生资源微生物转化技术。先后主持或参加了18项国家或省部级以上科研项目。选育出的青霉抗降解物阻遏突变株,产酶能力达到了国际先进水平,已用于投资建厂生产饲料、食品加工、纺织和造纸工业用酶。主要论文及专著 与他人合作,在国内外学术期刊上发表论文200余篇,其中SCI收录刊物54篇。主编《生物工艺技术学》、现代微生物技术丛书(六册),参编《微生物学词典》《微生物生长与发酵工程》等著作。主要获奖 1."青霉纤维素酶系的酶学研究"获得了国家教委1987年科技进步二等奖。 2."纤维素酶系酶解机制和活力测定方法的研究"山东省1991年科技进步二等奖。 3."纤维素酶制剂"获山东省1997年科技进步二等奖。 4."纤维废物液体深层发酵生产纤维素酶"获国家教委1997年科技进步一等奖(发 明类)和1998年国家发明四等奖。 5."微生物对天然纤维素的降解机制研究"获国家教委1998年科技进步一等奖。 6.“麦草浆的生物漂白和酶法改性”2003年山东省科学技术奖技术发明二等奖 7.“生物预处理处理麦草化学机械法的研究”2004年山东省科学技发明二等奖 8.“麦草浆的生物漂白和酶法改性”2005年国家科学技术进步奖二等奖 9. 1990年,中国科协授予第二届"中国青年科技奖"。 10. 1991年,国家教委、国务院学位委员会授予"做出突出贡献的中国博士学位获得者"称号 11. 1996年被国家教委评选列入《跨世纪优秀人才计划》。 12. 1997年获政府特殊津贴 13. 1997年获山东省拔尖人才称号。 14. 2000年被命名为“山东省十大杰出留学科技专家”。
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2216
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735
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成果数
11
曲音波, XIAO Zhizhuang, WANG Pan, QU Yinbo*, *, GAO Peiji, WANG Tianhong
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-1年11月30日
Cold-active enzymes have received little research attention although they are very useful in industries. Since the structure bases of cold adaptation of enzymes are still unclear, it is also very difficult to obtain cold adapted enzymes for industrial applications using routine protein engineering methods. In this study, we employed directed evolution method to randomly mutate a mesophilic cellulase, endoglucanase Ⅲ (EG Ⅲ) from Trichoderma reesei, and obtained a cold adapted mutant, designated as w-3. DNA sequence analyses indicate that w-3 is a truncated form of native EG III with a deletion of 25 consecutive amino acids at its C-terminus. Further examination of enzymatic kinetics and thermal stability shows that mutant w-3 has a higher Kcat value and becomes more thermolabile than its parent. In addition, activation energy of w-3 and wild type EGIII calculated from Arrhenius equation are 13.3kJ.mol-1 and 26.2kJ.mol-1, respectively. Therefore, the increased specific activity of w-3 at lower temperatures could be resulted from increased Kcat value and decreased activation energy.
cold adaptation, directed evolution, endoglucanase Ⅲ, Trichoderma reesei
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曲音波, Congfa Li a, b, Qiao Liu a, Di Ding a, Hongjie Cui c, Aiguo Ji c, Yinbo Qu a, *
,-0001,():
-1年11月30日
A bacterial strain BZS21 with enantioselective epoxide hydrolase activity to trans ethyl 3-phenylglycidate was screened. The strain was identified as Pseudomonas sp. The enantiomeric excess of the remaining epoxide, (2R, 3S) ethyl 3-phenylglycidate, was significantly influenced by the conditions of cultivation and kinetic resolution. With 1% sucrose as carbon source, 0.2% beef extract, 0.2% peptone and 1.5% urea as mixed nitrogen source, the strain produced epoxide hydrolase with the highest enantioselectivity. And (2R, 3S) ethyl 3-phenylglycidate was obtained with ee of 94.6% and yield of 26.2%.
Epoxide hydrolase, ethyl 3-phenylglycidate, kinetic resolution, enantioselectivity, asymmetric hydrolysis
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曲音波, XIAO Zhizhuang, GAO Peiji, QU Yinbo* & WANG Tianhong
,-0001,():
-1年11月30日
The DNA fragment encoding the cellulose binding domain of endoglucanase Ⅲ (CBDEG Ⅲ) from Trichoderma reesei was subcloned and expressed in E. coli. The CBDEG Ⅲ had a high affinity for cellulose. The morphological and structural changes of cellulose after treatment with CBDEG Ⅲ indicated a 17.0% decrease in number of hydrogen bonds and a 16.5% decrease in crystalline index. X-ray diffraction and IR spectra analyses indicated that the destabilization and breakage of the hydrogen bonds in crystalline cellulose accounted for the non-hydrolytic disruption of the structure of cellulose.
cellulose-binding domain, endoglucanase Ⅲ, Trichoderma reesei
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曲音波, Jing Chen, Xin Song, Hui Zhang, Yinbo Qu*
,-0001,():
-1年11月30日
main product was separated and purified by HPLC and characterized as sophorolipid by nuclear magnetic resonance (NMR) and mass spectroscopy (MS). This is the first report on sophorolipids produced from W. domercqiae. Subsequently, the cytotoxic effects of the sophorolipid on cancer cells of H7402, A549, HL60 and K562 were investigated by MTT assay. The results showed a dose dependent inhibition ratio on cell viability according to the drug concentration ≤62.5μg/ml. These findings suggested that the sophorolipid produced by W. domercqiae have anticancer activity.
Sophorolipid, Wickerhamiella domercqia, Human cancer cell, Anticancer activity
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曲音波, Congfa Li , , Qiao Liu , Xin Song, Di Ding , Aiguo Ji &Yinbo Qu , *
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-1年11月30日
A Pseudomonas sp. was isolated with enantioselective epoxide hydrolase activity to ethyl 3-phenylglycidate. Cells grown on sucrose and suspended in 10% DMF (v/v) as cosolvent produced (2R,3S) ethyl 3-phenylglycidate with 95% ee and 26% yield in 12h from 0.2% (w/v) of the racemate.
enantioselectivity, epoxide hydrolase, ethyl 3-phenylglycidate, kinetic resolution
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曲音波, Ting Wang, Qian Yu, Xi Zhang, Yinbo Qu *, Peiji Gao, Tianhong Wang
,-0001,():
-1年11月30日
Error-prone PCR was used to randomly mutate the endoglucanase (EG Ⅲ) gene of Trichoderma reesei followed by screening for clear-hole-forming colonies on carboxymethyl cellulose (CMC) plates at high pH. A mutant was selected with a shift of pH optimum from 4.8-5.0 to 5.4, and its specific enzyme activity decreased in low pH and increased in high pH. The sequencing of the mutant gene showed that the asparagine residue at 321 position was substituted by threonine. Two site-directed mutations, N321D and N321H, were designed to study the role of EG Ⅲ-321. It was discovered that the pH activity profiles of these two mutants had obvious change compared to the wild-type enzyme. It suggested that the residue at position 321 is a key amino acid residue in determining the pH-activity profile of the EG Ⅲ from T. reesei. The rule accorded with the alkali-tolerant mechanism of alkaliphilic cellulase K.
Trichoderma reesei, Endoglucanase Ⅲ, Directed evolution, Site-directed mutagenesis, Asparagine-321
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曲音波, Xiangmei Liu, Yinbo Qu ∗, Fan You, Ying Liu
Journal of Molecular Catalysis B: Enzymatic 18(2002)307-313,-0001,():
-1年11月30日
Asparagine (Asn)-71 of the xylanase (XYN) from Bacillus pumilus A-30 was found highly conserved in alkaline xylanases of family G/11. The mutated gene fragments containing different substitutions of Asn-71 was obtained by site-directed mutagenesis to study its role in the alkali-tolerant mechanism of xylanase. The xylanase activity was completely lost if Asn-71 residue was replaced by alkaline arginine (Arg) or lysine (Lys) residues, but obviously depressed with a shift in the pH optimum of the enzyme from 6.7 to 6.3 if substituted by serine (Ser) or aspartate (Asp) residues. No mutant with a shift of the pH optimum to a more basic value was found. Furthermore, N71D lost its activity in the alkaline pH range completely, while N71S did not lose as much as that of N71D. Except for Asn-71, the random mutagenesis to other residues of the xylanase was also studied. The alkali-tolerant mechanism of the xylanase was analyzed by their charged character, ionized state, and the hydrogen bond network of the residues surrounding the two catalytic residues on the basis of homology modeling of the mutated xylanases.
Alkali-tolerance, Xylanase, Site-directed mutagenesis, Asparagine-71, Homology modeling
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曲音波, X. Zhang , , J. Kong and Y. Qu
Journal of Applied icrobiology ISSN 1364-5072,-0001,():
-1年11月30日
Aims: The aim of this study was to investigate the properties of temperate bacteriophage of Lactobacillus fermentum, based on its morphology, restriction patterns, protein profile and the impact on the growth of host strain. Methods and Results: With Mitomycin C, seven temperate phages were induced from Lactobacilli derived from Chinese yogurt. The temperate phages induced belong to the most common Bradley' s group B, having hexagonal head and long, noncontractile tail. They were furthermore confirmed to be the same bacteriophage by identical restriction patterns. SDS–PAGE profile showed that the phage studied had one major structure protein about 31Æ9 kDa. The presence of the prophage influenced the cell shape and colony size of its lysogenic strain. Conclusions: The phage obtained had similar, but not complete identical properties with other L. fermentum phages reported. It influenced the growth behaviour of its lysogenic strain. Significance and Impact of the Study: This study provides some information about bacteriophages occurring in the Chinese yoghurt manufacture and contributes to our knowledge on the bacteriophage diversity in the dairy industry.
Lactobacillus fermentum,, lysogenic strain,, prophage-cured strain,, restriction patterns,, temperate bacteriophage,, 16S rDNA.,
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【期刊论文】A biocatalyst for pyruvate preparation from dl-lactate: lactate oxidase in a Pseudomonas sp.
曲音波, Jingsong Gu a, b, Ping Xu a, ∗, Yinbo Qu a
Journal of Molecular Catalysis B: Enzymatic 18(2002)299-305,-0001,():
-1年11月30日
For the purpose of producing pyruvate from dl-lactate by enzymatic methods, four microorganism strains that produce lactate oxidase (LOD) were screened and isolated from many soil samples. Among them, strain SM-6, which showed high potential for pyruvate production,was chosen for further research. Physiological studies and 16S rDNArelationship reveal that SM-6 belongs to Pseudomonas putida. The optimized pH and temperature of the enzyme-catalyzed reaction were pH 7.2, and 39℃, respectively. Low-concentration EDTA (1mM) could improve the stability of pyruvate and conversion ratio of lactate oxidase. Vmax and Km value for dl-lactate were 2.46 mol/(min mg) protein and 9.53mM, respectively. On preparation scale, cell-free extract from SM-6, containing 300mg/l of crude enzyme (4037U/ml lactate oxidase), could convert 66% of 116mM of dl-lactate into 76.6mM pyruvate in 18h, and 82% of substrate was transformed after 48 h, giving 95.0mM (10.5 mg/ml) of pyruvate. The ratio of product to biocatalyst was 34.8:1 (g/g).
Pyruvate, Lactate oxidase, dl-Lactate, Biocatalyst, Pseudomonas
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曲音波, Ying Wang , Wen-Long Shi , Xiang-Yong Liu , Yu Shen , Xiao-Ming Bao , ∗, Feng-Wu Bai & Yin-BoQu
Biotechnology Letters 26: 885-890, 2004.,-0001,():
-1年11月30日
To produce an industrial strain of Saccharomyces cerevisiae that metabolizes xylose, we constructed a rDNA integration vector and YIp integration vector, containing the xylose-utilizing genes, XYL1 and XYL2, which encode xylose reductase (XR) and xylitol dehydrogenase (XDH) from Pichia stipitis, and XKS1, which encodes xylulokinase (XK) from S. cerevisiae, with the G418 resistance gene KanMX as a dominant selectable marker. The rDNA results in integration of multiple copies of the target genes. The industrial stain of S. cerevisiae NAN-27 was transformed with the two integration vectors to produce two recombinant strains, S. cerevisiae NAN-127 and NAN-123. Upon transformation, multiple copies of the xylose-utilizing genes were integrated into the genome rDNA locus of S. cerevisiae. Strain NAN-127 consumed twice as much xylose and produced 39% more ethanol than the parent strain, while NAN-123 consumed 10% more xylose and produced 10% more ethanol than the parent strain over 94 h.
ethanol, industrial strain,, integrating plasmid, Saccharomyces cerevisiae, xylose
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