Skip to main content
Log in

Purification and characterization of extracellular chitinase from a novel strain Aspergillus fumigatus CS-01

  • Published:
Journal of Central South University of Technology Aims and scope Submit manuscript

Abstract

Twelve samples derived from different locations in south central area of China are treated by enrichment and spread-plate technique for initial screening. Seven chitinase-producing strains are isolated. The chitinase present in the culture supernatant of strain CS-01 possesses the maximum activity of 0.118 U/mL. Analysis of the morphological feature and the ITS rDNA sequence reveals that strain CS-01 belongs to Aspergillus fumigatus. Production of the chitinase is regulated by a inducible way and the maximum activity appears at 36 h in colloidal chitin culture. Purification of the chitinase is carried out by salting out, gel filtrate chromatography and anion exchange chromatography sequentially. Native-PAGE and SDS-PAGE indicate that the chitinase from A. fumigatus CS-01 is a monomer with the relative molecular mass estimated to be 4.50×104. Its maximum activity appears at pH 5 and 55 °C. The chitinase is stable at pH 4.0–7.5 and below 45 °C.

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

Access this article

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

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. RINAUDO M. Chitin and chitosan: Properties and applications [J]. Progress in Polymer Science, 2006, 31(7): 603–632.

    Article  Google Scholar 

  2. MAJETI N V, RAVI K. A review of chitin and chitosan applications [J]. Reactive and Functional Polymers, 2000, 46(1): 1–27.

    Article  Google Scholar 

  3. PRASHANTH K, THARANATHAN R. Chitin/chitosan: Modifications and their unlimited application potential—An overview [J]. Trends in Food Science & Technology, 2007, 18(3): 117–131.

    Article  Google Scholar 

  4. HIRANO S. Chitin and chitosan as novel biotechnological materials [J]. Polymer International, 1999, 48(8): 732–734.

    Article  Google Scholar 

  5. XING Rong-e, LIU Song, YU Hua-hua, GUO Zhan-yong, WANG Pi-bo, LI Cui-ping, LI Zhi-en, LI Peng-cheng. Salt assisted acid hydrolysis of chitosan to oligomers under microwave irradiation [J]. Carbohydrate Research, 2005, 340(13): 2150–2153.

    Article  Google Scholar 

  6. HIEN N, NAGASAWA N, THAM L, YOSHII F, DANG V H, MITOMO H, MAKUUCHI K, KUME T. Growth-promotion of plants with depolymerized alginates by irradiation [J]. Radiation Physics and Chemistry, 2000, 59(1): 97–101.

    Article  Google Scholar 

  7. ALLAN G, PEYRON M. Molecular weight manipulation of chitosan I: Kinetics of depolymerization by nitrous acid [J]. Carbohydrate Research, 1995, 277(2): 257–272.

    Article  Google Scholar 

  8. PANTALEONE D, YALPANI M, SCOLLAR M. Unusual susceptibility of chitosan to enzymatic hydrolysis [J]. Carbohydrate Research, 1992, 237(1): 325–332.

    Article  Google Scholar 

  9. BOLAR J P, NORELLI J L, WONG K W, HAYES C K, HARMAN G E, ALDWINCKLE H S. Expression of endochitinase from Trichoderma harzianum in transgenic apple increases resistance to apple scab and reduces vigor [J]. Phytopatholigy, 2000, 90(1): 72–77.

    Article  Google Scholar 

  10. ZIMAND G, ELAD Y. Efect of Trichoderma harizianum on Bollrylis cinerea pathogenicity [J]. Phytopatholigy, 1996, 86(5): 945–956.

    Google Scholar 

  11. TRACHUK L, REVINA L, SHEMYAKINA T. Chitinases of bacillus lichenfoumis B-6839: Isolation and properties [J]. Canadian Journal of Micrrobiology, 1996, 42(4): 307–315.

    Article  Google Scholar 

  12. XIAO Xiang, ZHOU Ying, WANG Feng-ping. Isolation and identification of a high-efficient chitin-degrading marine bacterium CB101 and studies on its chitinase system[J]. Acta Oceanologica Sinica, 2003, 25(1): 138–142. (in Chinese)

    Google Scholar 

  13. SHUTTON D, FOTHERQILL A, RINALDI M. Guide to clinically significant fungi [M]. Baltimore: Williams & Wilkins, 1998.

    Google Scholar 

  14. XIA Jin-lan, PENG An-an, HE Huan, YANG Yu, LIU Xue-duan, QIU Guan-zhou. A new strain acidithiobacillus albertensis BY-05 for bioleaching of metal sulfides ores [J]. Transactions of Nonferrous Metals Society of China, 2007, 17(1): 168–175.

    Article  Google Scholar 

  15. INNIS M A, GELFAND D H, SNINSKY J J, WHITE T J. PCR Protocols: A guide to methods and application [M]. San Diego, CA: Academic Press, 1990: 315–322.

    Google Scholar 

  16. RIVAS L A, PARRO V, MORENO-PAZ M. The Bacillus subtilis 168 csn gene encodes a chitosanase with similar properties to a streptomyces enzyme [J]. Microbiology, 2000, 146(1): 2929–2936.

    Google Scholar 

  17. WANG S L, CHEN Y H, WANG C L, YEN Y H, CHERN M K. Purification and characterization of a serine protease extracellularly produced by Aspergillus fumigatus in a shrimp and crab shell powder medium [J]. Enzyme and Microbial Technology, 2005, 36(5): 660–665.

    Article  Google Scholar 

  18. ESCOTT G M, HEAM V M, ADAMS D J. Inducible chitinolytic system of aspergillus fumigatus [J]. Microbiology, 1998, 144(6): 1575–1581.

    Article  Google Scholar 

  19. MARION M M. A rapid and sensitive method for the quantitation of protein utilizing the principle of protein-dye bindiag [J]. Analytical Biochemistry, 1976, 72: 248–254.

    Article  Google Scholar 

  20. UEDA H, ARAI M. Purification and some properties of chitinases from Aeromonas sp. No.10S-24 [J]. Bioscience, Biotechnology, and Biochemistry, 1992, 56: 460–464.

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Jin-lan Xia  (夏金兰).

Additional information

Foundation item: Projects(50621063, 50674101) supported by the National Natural Science Foundation of China

Rights and permissions

Reprints and permissions

About this article

Cite this article

Xia, Jl., Xiong, J., Xu, T. et al. Purification and characterization of extracellular chitinase from a novel strain Aspergillus fumigatus CS-01. J. Cent. South Univ. Technol. 16, 552–557 (2009). https://doi.org/10.1007/s11771-009-0092-5

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11771-009-0092-5

Key words

Navigation