Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Kinetics of Enriched Chitinase as Extracellular Metabolite in Beauveria bassiana

  • Received : 2018.02.12
  • Accepted : 2018.09.21
  • Published : 2019.03.28
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Abstract

Beauveria bassiana, one of the most common entomopathogenic fungi, has been isolated, pre defined and characterized in-house from soil of tea cultivation area. Experiments have been performed to verify the presence of chitinase as intracellular metabolite and its release as extracellular product rendering the spores with biopesticide activity. Although there are many responsible enzymes for the pest killer action of B. bassiana, binding property of chitinase depending on presence as well as absence of serine supplemented in the media has been studied with respect to the production and kinetics. A programmed investigation conclusively indicates that the isolated spore (hyphae) of B. bassiana has been metabolically enriched with the enzyme chitinase in presence of an externally added amino acid serine with its inhibitory kinetics.

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References

  1. Charnley AK. 2003. Fungal pathogens of insects: cuticle degrading enzymes and toxins. Adv. Botanical Res. 40: 241-321. https://doi.org/10.1016/S0065-2296(05)40006-3
  2. Zacharuk RY. 1970. Fine structure of the fungus Metarhizium anisopliae infecting three species of larval Elateridae.III. Penetration of the host integument. J. Invertebr. Pathol. 15: 372-396. https://doi.org/10.1016/0022-2011(70)90182-5
  3. Zhang J, Cai J, Wu K, Jin S, Pan R, Fan M. 2004. Production and properties of chitinase from Beauveria bassiana Bb174 in solid state fermentation. Ying Yong Sheng Tai Xue Bao. 15: 863-866.
  4. Fang W, Leng B, Xiao Y, Jin K, Ma J, Fan Y, et al. 2005. Cloning of Beauveria bassiana chitinase gene Bbchit1 and its application to improve Fungal strain virulence. Appl. Environ. Microbiol. 71: 363-370. https://doi.org/10.1128/AEM.71.1.363-370.2005
  5. Hayes CK, Klemsdal S, Lorito M, Di Pietro A, Peterbauer C, Nakas JP, et al. 1994. Isolation and sequence of an endochitinaseencoding gene from a cDNA library of Trichoderma harzianum. Gene. 138: 143-148. https://doi.org/10.1016/0378-1119(94)90797-8
  6. Seidl V, Huemer B, Seiboth B, Kubicek CP. 2005. A complete survey of Trichoderma chitinases reveals three distinct subgroups of family 18 chitinases. FEBS J. 272: 5923-5939. https://doi.org/10.1111/j.1742-4658.2005.04994.x
  7. Takaya N, Yamazaki D, Horiuchi H, Ohta A, Takagi M. 1998. Intracellular chitinase gene from Rhizopus oligosporus: molecular cloning and characterization. Microbiology 144: 2647-2654. https://doi.org/10.1099/00221287-144-9-2647
  8. Arakane Y, Zhu Q, Matsumiya M, Muthukrishnan S, Kramer KJ. 2003. Properties of catalytic, linker and chitin-binding domains of insect chitinase. Insect. Biochem. Mol. Biol. 33: 631-648. https://doi.org/10.1016/S0965-1748(03)00049-3
  9. Mondal S, Datta S, Mukherjee A, Bhattacharya P. 2015. Studies on isolation, optimization and bioprocess engineering behaviour of entomopathogenic fungi, Beauveria bassiana. Indian Chem. Eng. 59: 41-56.
  10. Narayana KJP, Vijayalakshmi M. 2009. Chitinase production by Streptomyces sp. ANU 627. Braz. J. Microbiol. 40: 725-733. https://doi.org/10.1590/S1517-83822009000400002
  11. Murthy N, Bleakley B. 2012. Simplified method of preparing colloidal chitin used for screening of chitinase- producing microorganisms. Int. J. Microbiol. 10: 2-7.
  12. Miller GP. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31: 426-428. https://doi.org/10.1021/ac60147a030
  13. Kuusk S, Bissaro B, Kuusk P, Forsberg Z, Eijsink VGH, Sorlie M, et al. 2018. Kinetics of $H_2O_2$-driven degradation of chitin by a bacterial lytic polysaccharide monooxygenase. J. Biol. Chem. 293: 523-531. https://doi.org/10.1074/jbc.M117.817593
  14. Nagpure A, Gupta R. 2013. Purification and characterization of an extracellular Chitinase from antagonistic Streptomyces violaceusniger. J. Basic Microbiol. 53: 429-439. https://doi.org/10.1002/jobm.201100648