Skip to main content
SpringerLink
Log in

Enhancement of Catalytic Performance of α-dextranase from Chaetomium gracile Through Optimization and Suitable Shear Force

  • Research Article
  • Published:
Sugar Tech Aims and scope Submit manuscript

Abstract

Dextran causes negative impact on the normal production of sugar industry. Traditional removal methods have many disadvantages. 6-alpha-d-glucan-6-glucanohydrolase (EC 3.2.1.11) from Chaetomium gracile without food safety concern could remove dextran, but it has low level of enzyme production. The present study aimed to improve α-dextranase activity to meet industry demand. Consequently, α-dextranase activity reached 242.8 U/mL when fermentation condition was 29 °C, pH 6.0 and 220 rpm. Meanwhile, ten glass beads were added to fermentation medium when fermentation time was 12 h, which improved enzyme activity by 135.5% with the highest activity. Purified α-dextranase exhibited excellent thermal stability and surfactants tolerance. α-Dextranase from C. gracile could remove dextran by 46.6% in mixed sugarcane juice and 14.1% in clarified sugarcane juice. It had similar dextran removal efficiency with commercial enzymes. These evaluations showed that α-dextranase had great potential in removing dextran in sugar industry.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6

Similar content being viewed by others

References

  • Abdel-Naby, M.A., A.-M.S. Ismail, A.M. Abdel-Fattah, and A.F. Abdel-Fattah. 1999. Preparation and some properties of immobilized Penicillium funiculosum 258 dextranase. Process Biochemistry 34: 391–398.

    Article  CAS  Google Scholar 

  • Ali, M.S., C.C. Yun, A.L. Chor, R.N. Rahman, M. Basri, and A.B. Salleh. 2012. Purification and characterisation of an F16L mutant of a thermostable lipase. Protein Journal 31: 229–237.

    Article  CAS  PubMed  Google Scholar 

  • Amorim, R.V.S., E.S. Melo, M.G. Carneiro-da-Cunha, W.M. Ledingham, and G.M. Campos-Takaki. 2003. Chitosan from Syncephalastrum racemosum used as a film support for lipase immobilization. Bioresoure Technology 89: 35–39.

    Article  CAS  Google Scholar 

  • Bashari, M., Z.Y. Jin, J.P. Wang, and X.B. Zhan. 2016. A novel technique to improve the biodegradation efficiency of dextranase enzyme using the synergistic effects of ultrasound combined with microwave shock. Innovative Food Science & Emerging Technologies 35: 125–132.

    Article  CAS  Google Scholar 

  • Boil, P.G.M.D. 1997. Refined sugar and floc formation. A survey of the literature. International Sugar Journal 99: 310–314.

    Google Scholar 

  • Chen, L., X.S. Zhou, W.M. Fan, and Y.X. Zhang. 2008. Expression, purification and characterization of a recombinant Lipomyces starkey dextranase in Pichia pastoris. Protein Expression and Purification 58: 87–93.

    Article  CAS  PubMed  Google Scholar 

  • Cheng, N., K. Koda, Y. Tamai, Y. Yamamoto, T.E. Takasuka, and Y. Uraki. 2017. Optimization of simultaneous saccharification and fermentation conditions with amphipathic lignin derivatives for concentrated bioethanol production. Bioresoure Technology 232: 126–132.

    Article  CAS  Google Scholar 

  • Deng, L., J.M. Qin, X.P. Jia, and X. Guo. 2017. Enhanced thermoelectric performance of skutterudites via orthogonal experimental design. Journal of Alloys and Compounds 695: 3152–3155.

    Article  CAS  Google Scholar 

  • Eggleston, G., and A. Monge. 2005. Optimization of sugarcane factory application of commercial dextranases. Process Biochemistry 40: 1881–1894.

    Article  CAS  Google Scholar 

  • Franssen, O., O.P. Vos, and W.E. Hennink. 1997. Delayed release of a model protein from enzymatically-degrading dextran hydrogels. Journal of Controlled Release 44: 237–245.

    Article  CAS  Google Scholar 

  • Fukumoto, J., H. Tsuji, and D. Tsuru. 1971. Studies on mold dextranases. I. Penicillium luteum dextranase: Its production and some enzymatic properties. Journal of Biochemistry 69: 1113–1121.

    Article  CAS  PubMed  Google Scholar 

  • Hayacibara, M.F., H. Koo, A.M. Vacca Smith, L.K. Kopec, K. Scott-Anne, J.A. Cury, and W.H. Bowen. 2004. The influence of mutanase and dextranase on the production and structure of glucans synthesized by streptococcal glucosyltransferases. Carbohydrate Research 339: 2127–2137.

    Article  CAS  PubMed  Google Scholar 

  • Hoang, N.X., S. Ferng, C.-H. Ting, W.-H. Huang, R.Y.-Y. Chiou, and C.-K. Hsu. 2016. Optimizing the initial moromi fermentation conditions to improve the quality of soy sauce. LWT-Food Science and Technology 74: 242–250.

    Article  Google Scholar 

  • Holman, B.W.B., S.M. Fowler, and D.L. Hopkins. 2016. Are shear force methods adequately reported? Meat Science 119: 1–6.

    Article  PubMed  Google Scholar 

  • Jiménez, E.R. 2009. Dextranase in sugar industry: A review. Sugar Tech 11: 124–134.

    Article  Google Scholar 

  • Khalikova, E., P. Susi, and T. Korpela. 2005. Microbial dextran-hydrolyzing enzymes: Fundamentals and applications. Microbiology and Molecular Biology Reviews 69: 306–325.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Li, K., H. Lu, F. Hang, S. Li, and J. Liu. 2016. Improved dextranase production by Chaetomium gracile through optimization of carbon source and fermentation parameters. Sugar Tech 19: 432–437. doi:10.1007/s12355-016-0476-4.

    Article  Google Scholar 

  • Nikhil, U.N., A.D. Carl, and H. Zhao. 2010. Engineering of enzymes for selective catalysis. Current Organic Chemistry 14: 1870–1882.

    Article  Google Scholar 

  • Patil, S.S., A. Kar, and D. Mohapatra. 2016. Stabilization of rice bran using microwave: Process optimization and storage studies. Food and Bioproducts Processing 99: 204–211.

    Article  CAS  Google Scholar 

  • Purushe, S., D. Prakash, N.N. Nawani, P. Dhakephalkar, and B. Kapadnis. 2012. Biocatalytic potential of an alkalophilic and thermophilic dextranase as a remedial measure for dextran removal during sugar manufacture. Bioresoure Technology 115: 2–7.

    Article  CAS  Google Scholar 

  • Robyt, J.F., and S.H. Eklund. 1982. Stereochemistry involved in the mechanism of action of dextransucrase in the synthesis of dextran and the formation of acceptor products. Bioorganic Chemistry 11: 115–132.

    Article  CAS  Google Scholar 

  • Virgen-Ortíz, J.J., V. Ibarra-Junquera, P. Escalante-Minakata, J.D.J. Ornelas-Paz, J.A. Osuna-Castro, and A. González-Potes. 2015. Kinetics and thermodynamic of the purified dextranase from Chaetomium erraticum. Journal of Molecular Catalysis. B, Enzymatic 122: 80–86.

    Article  Google Scholar 

  • Wang, D., M.S. Lu, S.J. Wang, Y.L. Jiao, W.J. Li, Q. Zhu, and J.P. Liu. 2014. Purification and characterization of a novel marine Arthrobacter oxydans KQ11 dextranase. Carbohydrate Polymers 106: 71–76.

    Article  CAS  PubMed  Google Scholar 

  • Wynter, C.V.A., M. Chang, J. De, B. Jersey, P.A.Inkerman Patel, and S. Hamilton. 1997. Isolation and characterization of a thermostable dextranase. Enzyme and Microbial Technology 20: 242–247.

    Article  Google Scholar 

  • Zhang, Z.D., D.M. Lan, P.F. Zhou, J. Li, B. Yang, and Y. Wang. 2017. Control of sticky deposits in wastepaper recycling with thermophilic esterase. Cellulose 24: 1–11.

    Article  Google Scholar 

  • Zhang, Z.D., J.D. Liu, H.Q. Lu, F.X. Hang, C.R. Shi, and K. Li. 2015. Study on the improvement effect of low- frequency ultrasonic on the production of α-dextranase in Chaetomium gracile. Science and Technology of Food Industry 5: 234–241.

    Google Scholar 

  • Zohra, R.R., A. Aman, R.R. Zohra, A. Ansari, M. Ghani, and S.A.U. Qader. 2013. Dextranase: Hyper production of dextran degrading enzyme from newly isolated strain of Bacillus licheniformis. Carbohydrate Polymers 92: 2149–2153.

    Article  CAS  PubMed  Google Scholar 

Download references

Acknowledgements

This work was supported by the National Natural Science Foundation of China (31460026, 31560027) and Guangxi Science and Technology Development Program (Grant No. 14122003-6).

Author information

Authors and Affiliations

  1. School of Light Industry and Food Engineering, Guangxi University, 100 Daxue Road, Nanning, 530004, Guangxi, China

    Zedong Zhang, Jidong Liu, Shaoying Ma, Haiqin Lu, Fangxue Hang, Peng Huang & Kai Li

  2. Engineering Center for Sugarcane and Cane Sugar, Guangxi University, 100 Daxue Road, Nanning, 530004, China

    Haiqin Lu, Fangxue Hang & Kai Li

  3. Collaborative Innovation Center, Guangxi University, 100 Daxue Road, Nanning, 530004, Guangxi, China

    Haiqin Lu, Fangxue Hang & Kai Li

  4. School of Food Science and Engineering, South China University of Technology, Guangzhou, 510640, China

    Zedong Zhang

Authors
  1. Zedong Zhang
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Jidong Liu
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Shaoying Ma
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Haiqin Lu
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Fangxue Hang
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Peng Huang
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. Kai Li
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Kai Li.

Ethics declarations

Conflict of interest

The authors confirm that there are no conflicts of interest regarding this paper.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Zhang, Z., Liu, J., Ma, S. et al. Enhancement of Catalytic Performance of α-dextranase from Chaetomium gracile Through Optimization and Suitable Shear Force. Sugar Tech 20, 78–87 (2018). https://doi.org/10.1007/s12355-017-0540-8

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12355-017-0540-8

Keywords

Search

Navigation