Cuiqing Ma

Shandong University, Chi-nan-shih, Shandong Sheng, China

Are you Cuiqing Ma?

Claim your profile

Publications (117)448.08 Total impact

  • Bo Yu · Fei Tao · Fuli Li · Jianfeng Hou · Hongzhi Tang · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: Mycobacterium goodii X7B appeared to have the ability to remove organic sulfur from a broad range of sulfur species in gasoline, diesel and crude oils. The predominant properties make it as a potential workhorse for petroleum biodesulfurization process. We sequenced and annotated the whole genome to serve as a basis for further elucidation of the genetic background of this promising strain, and provide opportunities for investigating the metabolic and regulatory mechanisms. Copyright © 2015. Published by Elsevier B.V.
    Journal of Biotechnology 08/2015; DOI:10.1016/j.jbiotec.2015.08.004 · 2.88 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: d-Lactate was identified as one of a few available organic acids that supported the growth of Gluconobacter oxydans 621H in this study. Interestingly, this strain used d-lactate as an energy source but not as a carbon source, unlike other lactate-utilizing bacteria. The enzymatic basis for the growth of G. oxydans 621H on d-lactate was therefore investigated. Although two putative NAD-independent d-lactate dehydrogenases, GOX1253 and GOX2071, were capable of oxidizing d-lactate, GOX1253 was the only enzyme able to support the d-lactate-driven growth of the strain. GOX1253 was characterized as a membrane-bound dehydrogenase with a high activity towards d-lactate, while GOX2071 was characterized as a soluble oxidase with broad substrate specificity towards d-2-hydroxy acids. The latter used molecular oxygen as a direct electron acceptor, a feature that has not been reported previously in d-lactate oxidizing enzymes. This study not only clarifies the mechanism for the growth of G. oxydans on d-lactate, but also provides new insights for applications of the important industrial microbe and the novel d-lactate oxidase. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Applied and Environmental Microbiology 04/2015; 81(12). DOI:10.1128/AEM.00527-15 · 3.95 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Diacetyl, a high value product that can be extensively used as a food ingredient, could be produced from the non-enzymatic oxidative decarboxylation of α-acetolactate during 2,3-butanediol fermentation. In this study, the 2,3-butanediol biosynthetic pathway in Enterobacter cloacae subsp. dissolvens strain SDM, a good candidate for microbial 2,3-butanediol production, was reconstructed for diacetyl production. To enhance the accumulation of the precursor of diacetyl, the α-acetolactate decarboxylase encoding gene (budA) was knocked out in strain SDM. Subsequently, the two diacetyl reductases DR-I (gdh) and DR-II (budC) encoding genes were inactivated in strain SDM individually or in combination to decrease the reduction of diacetyl. Although the engineered strain E. cloacae SDM (ΔbudAΔbudC) was found to have a good ability for diacetyl production, more α-acetolactate than diacetyl was produced simultaneously. In order to enhance the nonenzymatic oxidative decarboxylation of α-acetolactate to diacetyl, 20 mM Fe(3+) was added to the fermentation broth at the optimal time. In the end, by using the metabolically engineered strain E. cloacae SDM (ΔbudAΔbudC), diacetyl at a concentration of 1.45 g/L was obtained with a high productivity (0.13 g/(L·h)). The method developed here may be a promising process for biotechnological production of diacetyl.
    Scientific Reports 03/2015; 5:9033. DOI:10.1038/srep09033 · 5.58 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Biotechnological production of biofuels is restricted by toxicity of the products such as ethanol and butanol. As its low toxicity to microbes, 2,3-butanediol (2,3-BD), a fuel and platform bio-chemical, could be a promising alternative for biofuel production from renewable bioresources. In addition, no bacterial strains have been reported to produce enantiopure 2,3-BD using lignocellulosic hydrolysates. In this study, Enterobacter cloacae strain SDM was systematically and metabolically engineered to construct an efficient biocatalyst for production for the fuel and enantiopure bio-chemical-(2R,3R)-2,3-BD. First, the various (2R,3R)-2,3-BD dehydrogenase encoding genes were expressed in a meso-2,3-BD dehydrogenase encoding gene disrupted E. cloacae strain under native promoter Pb of the 2,3-BD biosynthetic gene cluster of E. cloacae. Then, carbon catabolite repression was eliminated via inactivation of the glucose transporter encoding gene ptsG and overexpression of a galactose permease encoding gene galP. The resultant strain could utilize glucose and xylose simultaneously. To improve the efficiency of (2R,3R)-2,3-BD production, the byproduct-producing genes (ldh, frdA, and adh) were knocked out, thereby enhancing the yield of (2R,3R)-2,3-BD by 16.5% in 500-mL Erlenmeyer flasks. By using fed-batch fermentation in a 5-L bioreactor, 152.0g/L (2R,3R)-2,3-BD (purity>97.5%) was produced within 44h with a specific productivity of 3.5g/[L·h] and a yield of 97.7% from a mixture of glucose and xylose, two major carbohydrate components in lignocellulosic hydrolysates. In addition, when a lignocellulosic hydrolysate was used as the substrate, 119.4g/L (2R,3R)-2,3-BD (purity>96.0%) was produced within 51h with a productivity of 2.3g/[L·h] and a yield of 95.0%. These results show that the highest records have been acquired for enantiopure (2R,3R)-2,3-BD production by a native or engineered strain from biomass-derived sugars. In addition to producing the 2,3-BD, our systematic approach might also be used in the production of other important chemicals by using lignocellulose-derived sugars. Copyright © 2014. Published by Elsevier Inc.
    Metabolic Engineering 12/2014; 28. DOI:10.1016/j.ymben.2014.11.010 · 8.26 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: As an important method for building blocks synthesis, whole cell biocatalysis is hindered by some shortcomings such as unpredictability of reactions, utilization of opportunistic pathogen, and side reactions. Due to its biological and extensively studied genetic background, Pseudomonas putida KT2440 is viewed as a promising host for construction of efficient biocatalysts. After analysis and reconstruction of the lactate utilization system in the P. putida strain, a novel biocatalyst that only exhibited NAD-independent d-lactate dehydrogenase activity was prepared and used in l-2-hydroxy-carboxylates production. Since the side reaction catalyzed by the NAD-independent l-lactate dehydrogenase was eliminated in whole cells of recombinant P. putida KT2440, two important l-2-hydroxy-carboxylates (l-lactate and l-2-hydroxybutyrate) were produced in high yield and high optical purity by kinetic resolution of racemic 2-hydroxy carboxylic acids. The results highlight the promise in biocatalysis by the biotechnologically important organism P. putida KT2440 through genomic analysis and recombination.
    Scientific Reports 11/2014; 4:6939. DOI:10.1038/srep06939 · 5.58 Impact Factor
  • Chao Gao · Zhong Li · Lijie Zhang · Chao Wang · Kun Li · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: Conversion of glycerol into high-value products is of significant importance for sustainability in the biofuel industry. In this study, pyruvic acid, a central intermediate needed for the production of versatile biomolecules, was produced from glycerol without the addition of any cofactors by the cell-free bio-system composed of alditol oxidase, dihydroxy acid dehydratase, and catalase. (3R)-Acetoin was then produced at 85.5% of the theoretical yield from glycerol by α-acetolactate synthase and α-acetolactate decarboxylase. Since other biomolecules can also be produced from pyruvic acid, the cell-free bio-system might serve as a versatile bio-production platform, and support the viability of the biofuel economy.
    Green Chemistry 11/2014; 17(2). DOI:10.1039/C4GC01685H · 6.85 Impact Factor
  • Jiayang Qin · Xiuwen Wang · Jian Kong · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: In this study, a food-grade cell surface display host/vector system for Lactobacillus casei was constructed. The food-grade host L. casei Q-5 was a lactose-deficient derivative of L. casei ATCC 334 obtained by plasmid elimination. The food-grade cell surface display vector was constructed based on safe DNA elements from lactic acid bacteria containing the following: pSH71 replicon from Lactococcus lactis, lactose metabolism genes from L. casei ATCC 334 as complementation markers, and surface layer protein gene from Lactobacillus acidophilus ATCC 4356 for cell surface display. The feasibility of the new host/vector system was verified by the expression of green fluorescent protein (GFP) on L. casei. Laser scanning confocal microscopy and immunofluorescence analysis using anti-GFP antibody confirmed that GFP was anchored on the surface of the recombinant cells. The stability of recombinant L. casei cells in artificial gastrointestinal conditions was verified, which is beneficial for oral vaccination applications. These results indicate that the food-grade host/vector system can be an excellent antigen delivery vehicle in oral vaccine construction.
    Microbiological Research 09/2014; DOI:10.1016/j.micres.2014.02.001 · 1.94 Impact Factor
  • Lixiang Li · Chao Chen · Kun Li · Yu Wang · Chao Gao · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: 2,3-Butanediol (2,3-BD) is an important starting material for the manufacture of bulk chemicals. For efficient and large-scale production of 2,3-BD through fermentation, low-cost substrates are required. One such substrate, inulin, is a polydisperse fructan found in a wide variety of plants. In this study, a levanase with high inulinase activity and high pH and temperature stability was identified in Bacillus licheniformis strain ATCC 14580. B. licheniformis strain ATCC 14580 was found to efficiently produce 2,3-BD from fructose at 50°C. Then, the levanase was used for simultaneous saccharification and fermentation (SSF) of inulin to 2,3-BD. A fed-batch SSF yielded 103.0 g/liter 2,3-BD in 30 h, with a high productivity of 3.4 g/liter · h. The results suggest that the SSF process developed with the thermophilic B. licheniformis strain used might be a promising alternative for efficient 2,3-BD production from the favorable substrate inulin.
    Applied and Environmental Microbiology 08/2014; 80(20). DOI:10.1128/AEM.01802-14 · 3.95 Impact Factor
  • Source
    Lixiang Li · Kun Li · Kai Wang · Chao Chen · Chao Gao · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: In this study, a thermophilic Bacillus licheniformis strain X10 was newly isolated for 2,3-butanediol (2,3-BD) production from lignocellulosic hydrolysate. Strain X10 could utilize glucose and xylose simultaneously without carbon catabolite repression. In addition, strain X10 possesses high tolerance to fermentation inhibitors including furfural, vanillin, formic acid, and acetic acid. In a fed-batch fermentation, 74.0g/L of 2,3-BD was obtained from corn stover hydrolysate, with a productivity of 2.1g/Lh and a yield of 94.6%. Thus, this thermophilic B. licheniformis strain is a candidate for the development of efficient industrial production of 2,3-BD from corn stover hydrolysate.
    Bioresource Technology 08/2014; 170C:256-261. DOI:10.1016/j.biortech.2014.07.101 · 5.04 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Background (R)-2-Hydroxy-4-phenylbutyric acid [(R)-HPBA] is a key precursor for the production of angiotensin-converting enzyme inhibitors. However, the product yield and concentration of reported (R)-HPBA synthetic processes remain unsatisfactory. Methodology/Principal Findings The Y52L/F299Y mutant of NAD-dependent d-lactate dehydrogenase (d-nLDH) in Lactobacillus bulgaricus ATCC 11842 was found to have high bio-reduction activity toward 2-oxo-4-phenylbutyric acid (OPBA). The mutant d-nLDHY52L/F299Y was then coexpressed with formate dehydrogenase in Escherichia coli BL21 (DE3) to construct a novel biocatalyst E. coli DF. Thus, a novel bio-reduction process utilizing whole cells of E. coli DF as the biocatalyst and formate as the co-substrate for cofactor regeneration was developed for the production of (R)-HPBA from OPBA. The biocatalysis conditions were then optimized. Conclusions/Significance Under the optimum conditions, 73.4 mM OPBA was reduced to 71.8 mM (R)-HPBA in 90 min. Given its high product enantiomeric excess (>99%) and productivity (47.9 mM h−1), the constructed coupling biocatalysis system is a promising alternative for (R)-HPBA production.
    PLoS ONE 08/2014; 9(8):e104204. DOI:10.1371/journal.pone.0104204 · 3.23 Impact Factor
  • Source
    Pan Liu · Haiwei Zhang · Min Lv · Mandong Hu · Zhong Li · Chao Gao · Ping Xu · Cuiqing Ma
    [Show abstract] [Hide abstract]
    ABSTRACT: 5-Aminovalerate is a potential C5 platform chemical for synthesis of valerolactam, 5-hydroxyvalerate, glutarate, and 1,5-pentanediol. It is a metabolite of l-lysine catabolism through the aminovalerate pathway in Pseudomonas putida. l-Lysine monooxygenase (DavB) and 5-aminovaleramide amidohydrolase (DavA) play key roles in the biotransformation of l-lysine into 5-aminovalerate. Here, DavB and DavA of P. putida KT2440 were expressed, purified, and coupled for the production of 5-aminovalerate from l-lysine. Under optimal conditions, 20.8 g/L 5-aminovalerate was produced from 30 g/L l-lysine in 12 h. Because l-lysine is an industrial fermentation product, the two-enzyme coupled system presents a promising alternative for the production of 5-aminovalerate.
    Scientific Reports 07/2014; 4:5657. DOI:10.1038/srep05657 · 5.58 Impact Factor
  • Tianyi Jiang · Chao Gao · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: Lactate utilization endows microbes with the ability to use lactate as a carbon source. Lactate oxidizing enzymes play key roles in the lactate utilization pathway. Various types of these enzymes have been characterized, but novel ones remain to be identified. Lactate determination techniques and biocatalysts have been developed based on these enzymes. Lactate utilization has also been found to induce pathogenicity of several microbes, and the mechanisms have been investigated. More recently, studies on the structure and organization of operons of lactate utilization have been carried out. This review focuses on the recent progress and future perspectives in understanding microbial lactate utilization.
    Trends in Microbiology 06/2014; 22(10). DOI:10.1016/j.tim.2014.05.008 · 9.81 Impact Factor
  • Source
    Lixiang Li · Yu Wang · Kai Wang · Kun Li · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: Bacillus licheniformis strain 3F-3 is an efficient pentose-utilizing producer of platform chemical, 2,3-butanediol. Here we present a 4.1-Mb assembly of its genome. The key genes for pentose utilization, regulation, and metabolism of 2,3-butanediol were annotated, which may provide further insights into the molecular mechanism of 2,3-butanediol production from biomass pentose.
    Genome Announcements 05/2014; 2(3). DOI:10.1128/genomeA.00615-14
  • Source
    Lixiang Li · Yu Wang · Kun Li · Fei Su · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: Serratia marcescens strain ATCC 14041 was found to be an efficient meso-2,3-butanediol (meso-2,3-BD) producer from glucose and sucrose. Here we present a 5.0-Mb assembly of its genome. We have annotated 4 coding sequences (CDSs) for meso-2,3-BD fermentation and 2 complete operons including 6 CDSs for sucrose utilization.
    Genome Announcements 05/2014; 2(3). DOI:10.1128/genomeA.00590-14
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: The production of biofuels by recombinant Escherichia coli is restricted by the toxicity of the products. 2,3-Butanediol (2,3-BD), a platform and fuel bio-chemical with low toxicity to microbes, could be a promising alternative for biofuel production. However, the yield and productivity of 2,3-BD produced by recombinant E. coli strains are not sufficient for industrial scale fermentation. In this work, the production of 2,3-BD by recombinant E. coli strains was optimized by applying a systematic approach. 2,3-BD biosynthesis gene clusters were cloned from several native 2,3-BD producers, including Bacillus subtilis, Bacillus licheniformis, Klebsiella pneumoniae, Serratia marcescens, and Enterobacter cloacae, inserted into the expression vector pET28a, and compared for 2,3-BD synthesis. The recombinant strain E. coli BL21/pETPT7-EcABC, carrying the 2,3-BD pathway gene cluster from Enterobacter cloacae, showed the best ability to synthesize 2,3-BD. Thereafter, expression of the most efficient gene cluster was optimized by using different promoters, including PT7, Ptac, Pc, and Pabc. E. coli BL21/pET-RABC with Pabc as promoter was superior in 2,3-BD synthesis. On the basis of the results of biomass and extracellular metabolite profiling analyses, fermentation conditions, including pH, agitation speed, and aeration rate, were optimized for the efficient production of 2,3-BD. After fed-batch fermentation under the optimized conditions, 73.8 g/L of 2,3-BD was produced by using E. coli BL21/pET-RABC within 62 h. The values of both yield and productivity of 2,3-BD obtained with the optimized biological system were the highest ever achieved with an engineered E. coli strain. In addition to the 2,3-BD production, the systematic approach might also be used in the production of other important chemicals through recombinant E. coli strains.
    Metabolic Engineering 05/2014; 23. DOI:10.1016/j.ymben.2014.02.004 · 8.26 Impact Factor
  • Source
    Binbin Sheng · Jun Ni · Chao Gao · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: Gluconobacter oxydans strain DSM 2003 can efficiently produce some industrially important building blocks, such as (R)-lactic acid and (R)-2-hydroxybutyric acid. Here, we present a 2.94-Mb assembly of its genome sequence, which might provide further insights into the molecular mechanism of its biocatalysis in order to further improve its biotechnological applications.
    Genome Announcements 03/2014; 2(2). DOI:10.1128/genomeA.00417-14
  • Source
    Yujiao Wang · Chao Li · Chao Gao · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: Pseudomonas aeruginosa ATCC 15442 is an environmental strain of the Pseudomonas genus. Here, we present a 6.77-Mb assembly of its genome sequence. Besides giving insights into characteristics associated with the pathogenicity of P. aeruginosa, such as virulence, drug resistance, and biofilm formation, the genome sequence may provide some information related to biotechnological utilization of the strain.
    Genome Announcements 03/2014; 2(2). DOI:10.1128/genomeA.00421-14
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Bioethanol production from various starchy materials has received much attention in recent years. alpha-Amylases are key enzymes in the bioconversion process of starchy biomass to biofuels, food or other products. The properties of thermostability, pH stability, and Ca-independency are important in the development of such fermentation process. A novel Flavobacteriaceae Sinomicrobium alpha-amylase (FSA) was identified and characterized from genomic analysis of a novel Flavobacteriaceae species. It is closely related with archaeal alpha-amylases in the GH13_7 subfamily, but is evolutionary distant with other bacterial alpha-amylases. Based on the conserved sequence alignment and homology modeling, with minor variation, the Zn2+- and Ca2+-binding sites of FSA were predicated to be the same as those of the archaeal thermophilic alpha-amylases. The recombinant alpha-amylase was highly expressed and biochemically characterized. It showed optimum activity at pH 6.0, high enzyme stability at pH 6.0 to 11.0, but weak thermostability. A disulfide bond was introduced by site-directed mutagenesis in domain C and resulted in the apparent improvement of the enzyme activity at high temperature and broad pH range. Moreover, about 50% of the enzyme activity was detected under 100[degree sign]C condition, whereas no activity was observed for the wild type enzyme. Its thermostability was also enhanced to some extent, with the half-life time increasing from 25 to 55 minutes at 50[degree sign]C. In addition, after the introduction of the disulfide bond, the protein became a Ca-independent enzyme. The improved stability of FSA suggested that the domain C contributes to the overall stability of the enzyme under extreme conditions. In addition, successfully directed modification and special evolutionary status of FSA imply its directional reconstruction potentials for bioethanol production, as well as for other industrial applications.
    Biotechnology for Biofuels 01/2014; 7(1):18. DOI:10.1186/1754-6834-7-18 · 6.22 Impact Factor
  • Lixiang Li · Kun Li · Kai Wang · Chao Chen · Chao Gao · Cuiqing Ma · Ping Xu
    [Show abstract] [Hide abstract]
    ABSTRACT: In this study, a thermophilic Bacillus licheniformis strain X10 was newly isolated for 2,3-butanediol (2,3-BD) production from lignocellulosic hydrolysate. Strain X10 could utilize glucose and xylose simultaneously without carbon catabolite repression. In addition, strain X10 possesses high tolerance to fermentation inhibitors including furfural, vanillin, formic acid, and acetic acid. In a fed-batch fermentation, 74.0 g/L of 2,3-BD was obtained from corn stover hydrolysate, with a productivity of 2.1 g/L h and a yield of 94.6%. Thus, this thermophilic B. licheniformis strain is a candidate for the development of efficient industrial production of 2,3-BD from corn stover hydrolysate.
    Bioresource Technology 01/2014; 170:256–261. · 5.04 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: An NAD-dependent d-lactate dehydrogenase (d-nLDH) of Lactobacillus bulgaricus ATCC 11842 was rationally re-designed for asymmetric reduction of a homologous series of α-keto carboxylic acids such as phenylpyruvic acid (PPA), α-ketobutyric acid, α-ketovaleric acid, β-hydroxypyruvate. Compared with wild-type d-nLDH, the Y52L mutant d-nLDH showed elevated activities toward unnatural substrates especially with large substitutes at C-3. By the biocatalysis combined with a formate dehydrogenase for in situ generation of NADH, the corresponding (R)-α-hydroxy carboxylic acids could be produced at high yields and highly optical purities. Taking the production of chiral (R)-phenyllactic acid (PLA) from PPA for example, 50 mM PPA was completely reduced to (R)-PLA in 90 min with a high yield of 99.0% and a highly optical purity (>99.9% e.e.) by the coupling system. The results presented in this work suggest a promising alternative for the production of chiral α-hydroxy carboxylic acids.
    Scientific Reports 12/2013; 3:3401. DOI:10.1038/srep03401 · 5.58 Impact Factor

Publication Stats

2k Citations
448.08 Total Impact Points


  • 1997–2015
    • Shandong University
      • State Key Laboratory for Microbial Technology
      Chi-nan-shih, Shandong Sheng, China
  • 2008–2014
    • Shanghai Jiao Tong University
      • State Key Laboratory of Microbial Metabolism
      Shanghai, Shanghai Shi, China
  • 2011
    • Chinese Academy of Sciences
      • Institute of Microbiology
      Peping, Beijing, China
    • Wuhan Polytechnic University
      Wu-han-shih, Hubei, China
    • Helmholtz Centre for Infection Research
      Brunswyck, Lower Saxony, Germany