Production and characterization of chitooligosaccharides by the fungal chitinase Chit42 immobilized on magnetic nanoparticles and chitosan beads: selectivity, specificity and improved operational utility

Kidibule, Peter Elias; Costa, Jessica; Atrei, A.; Plou, Francisco J.; Fernández-Lobato, María; Pogni, Rebecca

doi:10.1039/d0ra10409d

Cited by 29 publications

(17 citation statements)

References 46 publications

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“…A chitinase immobilized on MNPs can be recovered easily, and can be used multiple times without losing much activity [ 99 ]. The immobilized enzyme is reported to be more active for COS production as compared to the free enzyme [ 97 ]. Different activators and cross-linking agents, such as 3-aminopropyl triethoxylsilane (APTES), cyanogen bromide, etc., are popularly used for the preparation of immobilized enzymes.…”

Section: Microbial Fermentation For Chitinase Productionmentioning

confidence: 99%

“…The molecular weight of the purified chitinases varies from 20 to 120 kDa, with a pI range from 4.5 to 8.5. Further, the efficiency and stability of purified free chitinases are generally less, which can be improved by immobilization [97]. Enzyme immobilization is used to achieve stable, reusable, and more active enzymes by the simple act of fixing an enzyme on a support surface [98].…”

Section: Purification Of Chitinasesmentioning

confidence: 99%

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Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Poria

Rana

Kumari

et al. 2021

Biology

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Chitinases are a large and diversified category of enzymes that break down chitin, the world’s second most prevalent polymer after cellulose. GH18 is the most studied family of chitinases, even though chitinolytic enzymes come from a variety of glycosyl hydrolase (GH) families. Most of the distinct GH families, as well as the unique structural and catalytic features of various chitinolytic enzymes, have been thoroughly explored to demonstrate their use in the development of tailor-made chitinases by protein engineering. Although chitin-degrading enzymes may be found in plants and other organisms, such as arthropods, mollusks, protozoans, and nematodes, microbial chitinases are a promising and sustainable option for industrial production. Despite this, the inducible nature, low titer, high production expenses, and susceptibility to severe environments are barriers to upscaling microbial chitinase production. The goal of this study is to address all of the elements that influence microbial fermentation for chitinase production, as well as the purifying procedures for attaining high-quality yield and purity.

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Section: Microbial Fermentation For Chitinase Productionmentioning

confidence: 99%

Section: Purification Of Chitinasesmentioning

confidence: 99%

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Poria

Rana

Kumari

et al. 2021

Biology

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“…Consequently, high variety of COS products, specially NAG2 and NAG3, were identified [20] . Recently, we attempted the immobilization of this enzyme on different supports and the effectiveness of the immobilized biocatalyst in the production of COS by the bioconversion of colloidal chitin and chitosan was evaluated [21] . In the present study, different protein variants of Chit42 were heterologously expressed in Pichia pastoris and three different complexes were obtained and analyzed using X-ray crystallography.…”

Section: Introductionmentioning

confidence: 99%

Structural inspection and protein motions modelling of a fungal glycoside hydrolase family 18 chitinase by crystallography depicts a dynamic enzymatic mechanism

Jiménez-Ortega

Kidibule

Fernández-Lobato

et al. 2021

Computational and Structural Biotechnology Journal

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“…At high pH, the alginate matrix may protect the enzyme from denaturation. Trichoderma harzianum Chit42 immobilised chitinase performed best at pH 4 (9) .…”

Section: Characterization Of Soluble and Immobilised Chitinasementioning

confidence: 99%

“…3). Similarly, Trichoderma harzianum Chit42 immobilised chitinase on chitosan beads had an optimum temperature of 45 • C (9) .…”

Section: Characterization Of Soluble and Immobilised Chitinasementioning

confidence: 99%

Kurthia gibsonii Mb126 immobilised chitinase against Aspergillus flavus, a fungal pathogen linked to lemon postharvest deterioration

Paul¹,

Mini²,

Benn³

et al. 2022

IJST

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Background of the study: As fungi become resistant to commonly used pesticides, fungicides are becoming not only more expensive, but also less effective in controlling postharvest infections. New chitinase immobilisation techniques are urgently needed to minimize enzyme costs while enhancing bio catalytic performance, antifungal activity, enzyme stability, and reusability. Objectives: The objective of this study was to immobilise chitinase of Kurthia gibsonii Mb126 by entrapping it in calcium alginate beads and to analyse its antifungal activities against Aspergillus flavus. Methods: The optimal parameters influencing the immobilization process and the characteristics of soluble and immobilised chitinase of K. gibsonii Mb126 were analysed. The antifungal activities of immobilised and free chitinase of K. gibsonii Mb126 against A. flavus, which was isolated from decayed lemon fruit, were performed using the agar-disk diffusion method. Free chitinase 25.0 mL (0.8 U/mL) and immobilised chitinase 0.06 g (specific activity 124-192 U/mg) were treated on separate lemon fruits for testing antifungal activity against A. flavus. Findings: K. gibsonii Mb126 chitinase was immobilised perfectly in calcium alginate beads. After optimising process parameters of immobilisation (sodium alginate concentration 3%, calcium chloride 0.2 M, 120 min. curing time), the specific activity of K. gibsonii Mb126 immobilised chitinase improved to 11.9-fold greater than the free form of chitinase and the immobilisation yield increased to 84%. It was observed that the thermal stability and storage stability of immobilised chitinase were better than those of free enzymes. The immobilised chitinase could be reused, and it retained 78% activity even after 16 cycles. The surface morphology of immobilised chitinase was observed in a scanning electron microscope at different magnification powers. Enzyme kinetics was studied and compared with that of its chitinase soluble counterpart. An in vitro study demonstrated that immobilised chitinase of K. gibsonii Mb126 has higher antifungal activity against A. flavus. In vivo experimental study of the https://www.indjst.org/ 136

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Production and characterization of chitooligosaccharides by the fungal chitinase Chit42 immobilized on magnetic nanoparticles and chitosan beads: selectivity, specificity and improved operational utility

Abstract: Chitin-active enzymes are of great biotechnological interest due to the wide industrial application of chitinolytic materials.

Cited by 29 publications

References 46 publications

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Structural inspection and protein motions modelling of a fungal glycoside hydrolase family 18 chitinase by crystallography depicts a dynamic enzymatic mechanism

Kurthia gibsonii Mb126 immobilised chitinase against Aspergillus flavus, a fungal pathogen linked to lemon postharvest deterioration

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