Abstract
It has been planned to minimize the yield and quality impairment of the seed corn, which is strategically important in the world, by pests under storage conditions with a biological product produced with a biotechnological approach. In this context, the present study aimed to control the maize weevil Sitophilus zeamais, known as a warehouse pest, using a nanoformulation. In the study, the chitinase enzyme from Lactobacillus coryniformis was purified first using ammonium sulfate precipitation and then by using the HiTrap Capto DEAE column, and the molecular mass of the purified enzyme was determined to be ~ 33 kDa, and the optimum pH and the values as pH 6.0 and 65–75 °C, respectively. Five different doses of nanoformulation (2, 4, 6, 8 and 10 mg/L) were applied to corn grains by the spraying method with three repetitions so that the insect can ingest the formulation through feeding. The effects of the applications on the death rate and mean time of death of Sitophilus zeamais were determined. According to these findings, it was concluded that the best practice was nanoformulation with 6 mg/L, considering both the mortality rate (100%) and the average death time (2.4 days). Chitinase from L. coryniformis is a promising candidate for corn lice control and management.
Graphic abstract
Similar content being viewed by others
Data availability
All data and materials are available from the corresponding author.
References
Ahmad R, Sardar M (2014) Immobilization of cellulase on TiO2 nanoparticles by physical and covalent methods: a comparative study. Indian J Biochem Biophys 51:314–320
Anonymous (2020) Plant pests standard drug trial methods. https://www.tarimorman.gov.tr/TAGEM/Belgeler/yayin/Ambar%20Zararl%C4%B1lar%C4%B1%20Standart%20%20%C4%B0la%C3%A7%20Deneme%20Metotlar%C4%B1.pdf. Accessed 20 July 2020
Athanassiou CG, Kavallieratos NG, Benelli G, Losic D, Usha Rani P, Desneux N (2017) Nanoparticles for pest control: current status and future perspectives. J Pest Sci 91:1–15. https://doi.org/10.1007/s10340-017-0898-0
Binod P, Sukumaran RK, Shirke SV, Rajpu JC, Pandey A (2007) Evaluation of fungal culture filtrate containing chitinase as a biocontrol agent against Helicoverpa armigera. J Appl Microbiol 103:1845–1852. https://doi.org/10.1111/j.1365-2672.2007.03428.x
Boyer S, Zhang H, Lempérière G (2012) A review of control methods and resistance mechanisms in stored-product insects. Bull Entomol Res 102:213–229. https://doi.org/10.1017/S0007485311000654
Chen Y, Ding H, Sun S (2017) Preparation and characterization of ZnO nanoparticles supported on amorphous SiO2. Nanomaterials 7:217. https://doi.org/10.3390/nano7080217
Dahiya N, Tewari R, Hoondal GS (2006) Biotechnological aspects of chitinolytic enzymes: a review. Appl Microbiol Biotechnol 71:773–782. https://doi.org/10.1007/s00253-005-0183-7
Delfini CD, Villegas LB, Martínez MA, Baigorí MD (2021) Extracellular antifungal activity of chitinase-producing bacteria isolated from guano of insectivorous bats. Curr Microbiol 78:2787–2798. https://doi.org/10.1007/s00284-021-02555-0
Du J, Duan S, Miao J, Zhai M, Cao Y (2020) Purification and characterization of chitinase from Paenibacillus sp. Appl Biochem Biotechnol 164:77–88. https://doi.org/10.1002/bab.1889
Ertürk S, Yılmaz A, Fırat-Akdeniz T, Alkan M (2017) Fumigant effect of trans-anethole and carbon dioxide mixture against to Rhyzopertha dominica, Tribolium castaneum and Sitophilus oryza. Plant Prot Bull 57:391–400. https://doi.org/10.16955/bitkorb.320138
Gomaa EZ (2021) Microbial chitinases: properties, enhancement and potential applications. Protoplasma 258(4):695–710. https://doi.org/10.1007/s00709-021-01612-6
Hamsina H, Tang M, Hasani EIR (2021) Activity test, selectivity, stability of chitinase on amobil chitosan membranes. Int J Multicult Multirelig Underst 8:453–464. https://doi.org/10.18415/ijmmu.v8i7.2750
Hart PJ, Pfluger HD, Monzingo AF, Hollis T, Robertus JD (1995) The refined crystal structure of an endochitinasefrom Hordeum vulgare L. seeds at 1.8 Å resolution. J Mol Biol 248:402–413. https://doi.org/10.1016/S0022-2836(95)80059-X
Heap I (2014) Global perspective of herbicide-resistant weeds. Pest Manag Sci 70:1306–1315. https://doi.org/10.1002/ps.3696
Ismail SA, Hassan ME, Hashem AM (2019) Single step hydrolysis of chitin using thermophilic immobilized exochitinase on carrageenan-guar gum gel beads. Biocatal Agric Biotechnol 21:101281. https://doi.org/10.1016/j.bcab.2019.101281
Jameel M, Shoeb M, Khan MT, Ullah R, Mobin M, Farooqi MK, Adnan SM (2020) Enhanced insecticidal activity of thiamethoxam by zinc oxide nanoparticles: a novel nanotechnology approach for pest control. ACS Omega 5:1607–1615. https://doi.org/10.1021/acsomega.9b03680
Kasthuri N, Hayworth K, Lichtman J, Erdman N, Ackerley CA (2007) New technique for ultra-thin serial brain section imaging using scanning electron microscopy. Microsc Microanal 13(S02):26–27. https://doi.org/10.1017/S1431927607078002
Kidibule PE, Costa J, Atrei A, Plou FJ, Fernandez-Lobato M, Pogni R (2021) Production and characterization of chitooligosaccharides by the fungal chitinase Chit42 immobilized on magnetic nanoparticles and chitosan beads: selectivity, specificity and improved operational utility. RSC Adv 11:5529–5536. https://doi.org/10.1039/d0ra10409d
Kudan S, Pichyangkura R (2009) Purification and characterization of thermostable chitinase from Bacillus licheniformis SK-1. Appl Biochem Biotech 157:23–35. https://doi.org/10.1007/s12010-008-8328-7
Kumar J, Ramlal A, Mallick D, Mishra V (2021) An Overview of some biopesticides and their importance in plant protection for commercial acceptance. Plants 10:1185. https://doi.org/10.3390/plants10061185
Kurnaz-Yetim N, Hasanoğlu Özkan E, Sarı N (2019) Enzyme immobilization and optimization on polymeric nanospheres. Suleyman Demirel Univ J Sci 14:97–104. https://doi.org/10.29233/sdufeffd.479246
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685. https://doi.org/10.1038/227680a0
Laribi-Habchi H, Bouacem K, Allala F, Jabeur F, Selama O, Mechri S, Yahiaoui M, Bouanane-Darenfed A, Jaouadi B (2020) Characterization of chitinase from Shewanella inventionis HE3 with bio-insecticidal effect against granary weevil, Sitophilus granarius Linnaeus (Coleoptera: Curculionidae). Process Biochem 97:222–233. https://doi.org/10.1016/j.procbio.2020.06.023
Lee YS, Park IH, Yoo JS, Chung SY, Lee YC, Cho YS, Ahn SC, Kim CM, Choi YL (2007) Cloning, purification, and characterization of chitinase from Bacillus sp. DAU101. Bioresour Technol 98:2734–2741. https://doi.org/10.1016/j.biortech.2006.09.048
Lin CC, Li YY (2009) Synthesis of ZnO nanowires by thermal decomposition of zinc acetate dihydrate. Mater Chem Phys 113:334–337. https://doi.org/10.1016/j.matchemphys.2008.07.070
Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (2014) The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res 42(D1):D490–D495. https://doi.org/10.1093/nar/gkt1178
Loni PP, Patil JU, Phugare SS, Bajekal SS (2014) Purification and characterization of alkaline chitinase from Paenibacillus pasadenensis NCIM 5434. J Basic Microbiol 54(10):1080–1089. https://doi.org/10.1002/jobm.201300533
Magnusson J, Schnurer J (2001) Lactobacillus coryniformis subsp. coryniformis strain Si3 produces a broad-spectrum proteinaceous antifungal compound. Appl Environ Microbiol 67(1):1–5. https://doi.org/10.1128/aem.67.1.1-5.2001
Mohamed S, Bouacem K, Mechri S, Addou NA, Laribi-Habchi H, Fardeau ML, Jaouadi B, Darenfed AB, Hacène H (2019) Purification and biochemical characterization of a novel acido-halotolerant and thermostable endochitinase from Melghiribacillus thermohalophilus strain Nari2AT. Carbohydr Res 473:46–56. https://doi.org/10.1016/j.carres.2018.12.017
Mohammadzadeh R, Arazpour A, Akbari A (2020) Synthesis and characterisation of magnetic κ-carrageenan nanocomposites for chitinase33 enzyme immobilisation. Int J Nano Biomaterials 9(3–4):171–187. https://doi.org/10.1504/IJNBM.2020.112235
Moharram AM, Abdel-Galil FA, Hafez WMM (2021) On the enzymes’ actions of entomopathogenic fungi against certain indigenous and invasive insect pests. Egypt J Biol Pest Control 31:51. https://doi.org/10.1186/s41938-021-00397-3
Muzemu S, Chitamba J, Mutetwa B (2013) Evaluation of Eucalyptus tereticornis, Tagetes minuta and Carica papaya as stored maize grain protectants against Sitophilus zeamais (Motsch.) (Coleoptera: Curculionidae). Agric Fish 2(5):196–201. https://doi.org/10.11648/j.aff.20130205.13
Ojo JA, Omoloye AA (2016) Development and Life History of Sitophilus zeamais (Coleoptera: Curculionidae) on Cereal Crops. Adv Agric 2016:1–8. https://doi.org/10.1155/2016/7836379
Ong LGA, Lam HK, Lim MY, Tan TX (2017) Process optimization on chitinase production by locally isolated Enterobacter sp. and Zymomonas sp. Int J Chem Eng Appl 8(4):286–289. https://doi.org/10.18178/ijcea.2017.8.4.671
Pasin TM, de Oliveira TB, Scarcella ASDA, Polizeli MDLTDM, Guazzaroni ME (2021) Perspectives on expanding the repertoire of novel microbial chitinases for biological control. J Agric Food Chem 69(11):3284–3288. https://doi.org/10.1021/acs.jafc.1c00219
Patil NS, Jadhav JP (2015) Significance of Penicillium ochrochloron chitinase as a biocontrol agent against pest Helicoverpa armigera. Chemosphere 128:231–235. https://doi.org/10.1016/j.chemosphere.2015.01.038
Pour SA, Zibaee A, Rostami MG, Hoda H, Shahriari M (2021) Mortality and immune challenge of a native isolate of Beauveria bassina against the larvae of Glyphodes pyloalis Walker (Lepidoptera: Pyralidae). Egypt J Biol Pest Control 31:37. https://doi.org/10.1186/s41938-021-00386-6
Prasad M, Palanivelu P (2014) A novel method for the immobilization of a thermostable fungal chitinase and the properties of the immobilized enzyme. Biotechnol Appl Biochem 61(4):441–445. https://doi.org/10.1002/bab.1179
Preety HV (2017) Increasing the efficiency of immobilization and chitin determination using copper oxide nanoparticles. Talanta 168:246–256. https://doi.org/10.1016/j.talanta.2017.03.038
Preety HV (2018) A novel polyurethane/nano ZnO matrix for immobilization of chitinolytic enzymes and optical sensing of chitin. Int J Biol Macromol 106:1173–1183. https://doi.org/10.1016/j.ijbiomac.2017.08.114
Ramanaviciene A, Schuhmann W, Ramanavicius A (2006) AFM study of conducting polymer polypyrrole nanoparticles formed by redox enzyme–glucose oxidase–initiated polymerisation. Colloids Surf B Biointerfaces 48(2):159–166. https://doi.org/10.1016/j.colsurfb.2006.02.002
SAS Institute (2011) The SAS system for Windows. Release 9.3. SAS Inst; Cary, NC
Sachdeva V, Hooda V (2015) Immobilization of nitrate reductase onto epoxy affixed silver nanoparticles for determination of soil nitrates. Int J Biol Macromol 79:240–247. https://doi.org/10.1016/j.ijbiomac.2015.04.072
Sarıbuğa E, Dikbas N, Nadaroglu H, Şenol M, Cetin B (2014) Partial purification, characterization of phytase enzyme from Lactobacillus acidophilus Bacteria and determination of it’s some kinetic properties. J Pure Appl Microbiol 8:91–96
Shivakumar S, Karmali AN, Ruhimbana C (2014) Partial purification, characterization, and kinetic studies of a low-molecular-weight, alkali-tolerant chitinase enzyme from Bacillus subtilis JN032305, A potential biocontrol strain. Prep Biochem Biotechnol 44(6):617–632. https://doi.org/10.1080/10826068.2013.844708
Singh R, Upadhyay SK, Singh M, Sharma I, Sharma P, Kamboj P, Saini A, Voraha R, Sharma AK, Upadhyay TK, Khan F (2021) Chitin, chitinases and chitin derivatives in biopharmaceutical, agricultural and environmental perspective. Biointerface Res Appl Chem 11(3):9985–10005. https://doi.org/10.33263/BRIAC113.998510005
Sosnowska ME, Jankiewicz U, Kutwin M, Chwalibog A, Gałązka A (2018) Influence of salts and metal nanoparticles on the activity and thermal stability of a recombinant chitinase from Stenotrophomonas maltophilia N4. Enzyme Microb Technol 116:6–15. https://doi.org/10.1016/j.enzmictec.2018.05.003
Supernak-Marczewska M, Zielinski A (2020) Effects of the origin and deacetylation degree of chitosan on properties of its coatings on titanium. Coatings 10(2):99. https://doi.org/10.3390/coatings10020099
Vaidya R, Roy S, Macmil S, Gandhi S, Vyas P, Chhatpar HS (2003) Purification and characterization of chitinase from Alcaligenes xylosoxydans. Biotechnol Lett 25(9):715. https://doi.org/10.1023/A:1023406630791
Xavier R, Rekha K, Bairy K (2004) Health perspective of pesticide exposure and dietary management. Malays J Nutr 10(1):39–51
Xi H, Yu J, Sun Q, Lu J, Gu T, Guo X, Lia B, Chena X, Zhanga K, Kong W, Wu Y (2018) Expression and purification of pneumococcal surface protein a of clade 4 in Escherichia coli using hydroxylapatite and ion-exchange column chromatography. Protein Expr Purif 151:56–61. https://doi.org/10.1016/j.pep.2018.06.008
Xie XH, Fu X, Yan XY, Peng WF, Kang LX (2021) A Broad-specificity chitinase from penicillium oxalicum k10 exhibits antifungal activity and biodegradation properties of chitin. Mar Drugs 19(7):356. https://doi.org/10.3390/md19070356
Yahiaoui M, Laribi-Habchi H, Bouacem K, Asmani KL, Mechri S, Harir M, Bendif H, Aïssani-El Fertas R, Jaouadi B (2019) Purification and biochemical characterization of a new organic solvent-tolerant chitinase from Paenibacillus timonensis strain LK-DZ15 isolated from the Djurdjura Mountains in Kabylia. Algeria Carbohydr Res 483:107747. https://doi.org/10.1016/j.carres.2019.107747
Zhang P, Tan W (2001) Atomic force microscopy for the characterization of immobilized enzyme molecules on biosensor surfaces. Fresenius J Anal Chem 369(3–4):302–307. https://doi.org/10.1007/s002160000624
Zhu L, Chen L, Shao X, Cheng J, Yang Q, Qian X (2021) Novel inhibitors of an insect pest chitinase: design and optimization of 9-O-aromatic and heterocyclic esters of berberine. J Agric Food Chem 69(27):7526–7533. https://doi.org/10.1021/acs.jafc.0c07401
Acknowledgements
The authors would like to thank the The Scientific and Technological Research Council of Turkey (TÜBİTAK) for their financial support.
Funding
This work was supported by the The Scientific and Technological Research Council of Turkey (TÜBİTAK) (Grant Numbers 118O979).
Author information
Authors and Affiliations
Contributions
ND and SU conceived and designed research. ND, SU, GT and TÖÖ conducted experiments. ND, TÖÖ, GT and RK analyzed data. ND and SU wrote the manuscript. All authors read and approved the manuscript.
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that they have no conflict of interest.
Ethical approval
This research did not involve any studies with human participants or vertebrate research subjects.
Consent for publication
All authors have read and approved the final version.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Dikbaş, N., Uçar, S., Tozlu, G. et al. Bacterial chitinase biochemical properties, immobilization on zinc oxide (ZnO) nanoparticle and its effect on Sitophilus zeamais as a potential insecticide. World J Microbiol Biotechnol 37, 173 (2021). https://doi.org/10.1007/s11274-021-03138-8
Received:
Accepted:
Published:
DOI: https://doi.org/10.1007/s11274-021-03138-8