Myco-chitinases as versatile biocatalysts for translation of coastal residual resources to eco-competent chito-bioactives

Rajput, Meenakshi; Kumar, Manish; Pareek, Nidhi

doi:10.1016/j.fbr.2022.04.001

Cited by 6 publications

(7 citation statements)

References 118 publications

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“…The polymeric chains of chitin are organized as sheets grouped in parallel and/or anti parallel mode, giving different polymorphic structures named α, β and γ chitin [2]. Chitin is a biodegradable polymer that can be applied in several sectors such as textiles, cosmetics, paper and agriculture, among others [3]. Its polymeric structure can be enzymatically hydrolyzed by the action of chitinases to recover monomeric units, allowing for better collection of residues containing chitin, such as those produced by the fishing industry, such as shrimp, and minimizing the negative impact of residue accumulation in the environment.…”

Section: Introductionmentioning

confidence: 99%

“…The former randomly breaks down the β-1,4 linkage of chitin and chitodextrins to release N-acetylglucosamine and low molecular mass oligomers of β-1,4 Nacetylglucosamine such as chitobiose, chitotriose and chito-oligosaccharides (CHOS). The exochitinases are subdivided into two categories, the chitobiases (EC 3.2.1.29), promoting diacetylchitobiose from the non-reducing end from the chitin microfibrils, and β(1,4)Nacetylglucosaminidase (EC 3.2.1.30), acting on oligomeric products obtained by the action of the endochitinases and chitobiases, providing monomers of N-acetylglucosamine [3,4].…”

Section: Introductionmentioning

confidence: 99%

“…Among the microorganisms, the presence of chitinases is well documented in bacteria and fungi [5]. The fungal chitinases belong to the GH 18 family and present different physiological roles such as fungal growth, cell wall remodeling, mycoparasitism, autolysis and the use of chitin for nutritional and energy demands [3]. The fungal chitinases can be separated into three subgroups depending on the cleavage pattern (exo-/endo-), substratebinding cleft and the presence of carbohydrate-binding modules (CBMs).…”

Section: Introductionmentioning

confidence: 99%

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Purification, Characterization and Antifungal Activity of the Aspergillus niveus Chitinase Produced Using Shrimp Shells

Ornela,

Guimarães

2024

Applied Biosciences

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Chitinases are biotechnologically relevant enzymes that can be applied in such different sectors as pharmaceutical, food, environmental management, the biocontrol of pests and in the paper and cellulose industry. Microorganisms as filamentous fungi are the most important source of these biomolecules. The fungus Aspergillus niveus produces extracellular chitinase when cultured under submerged fermentation using shrimp shells, a residue generated by the fish industry, as a carbon source, for 96 h at 30 °C and 100 rpm. The particle size and concentration of the shrimp shells affected enzyme production. The chitinase was purified until electrophoretic homogeneity through the use of a Sephadex G-100 chromatographic column. It is a monomeric glycoprotein with a molecular mass of 47 kDa estimated using SDS-PAGE and 49.3 kDa determined using gel filtration. The carbohydrate content was 22.8%. The best temperature and pH for enzyme activity were 65 °C and 6.0, respectively. Approximately 80% of the enzymatic activity was preserved at pH 4.0 and 5.0 for 48 h, and the half-life (t50) was maintained for 48 h at 40 °C. Salts, EDTA and β-mercaptoethanol did not affect chitinase activity significantly, but organic solvents reduced it. The kinetic parameters determined using p-NPGlycNac were Km of 2.67 mmol L−1, Vmax of 12.58 U mg of protein−1, Kcat of 2.47 s−1 and K cat/Km of 0.93 s−1 mmol L−1. The A. niveus chitinase inhibited the growth of all fungal strains used, especially Trichoderma harzianum (MIC = 22.4 μg mL−1) and Penicillium purpurogenum (MIC = 11.2 μg mL−1). The chitinase produced by A. niveus presented interesting characteristics that indicate its potential of application in different areas.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Purification, Characterization and Antifungal Activity of the Aspergillus niveus Chitinase Produced Using Shrimp Shells

Ornela,

Guimarães

2024

Applied Biosciences

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“…The extracellular enzymatic compounds produced by EPF can degrade these chitinous compounds and obtain nutrients from the insect’s hemolymph 24 , 25 . The fungal chitinases usually belong to class 3 chitinases and are considered an important part of the family 18 of glycosyl hydrolases 26 . Fungal chitinases of family 18 contain a chitin-binding domain that efficiently depolarises chitin 27 , 28 .…”

Section: Introductionmentioning

confidence: 99%

Chitinase of Trichoderma longibrachiatum for control of Aphis gossypii in cotton plants

Anwar,

Amin,

Khan

et al. 2023

Sci Rep

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Chitinase-producing fungi have now engrossed attention as one of the potential agents for the control of insect pests. Entomopathogenic fungi are used in different regions of the world to control economically important insects. However, the role of fungal chitinases are not well studied in their infection mechanism to insects. In this study, Chitinase of entomopathogenic fungi Trichoderma longibrachiatum was evaluated to control Aphis gossypii. For this purpose, fungal chitinase (Chit1) gene from the genomic DNA of T. longibrachiatum were isolated, amplified and characterised. Genomic analysis of the amplified Chit1 showed that this gene has homology to family 18 of glycosyl hydrolyses. Further, Chit1 was expressed in the cotton plant for transient expression through the Geminivirus-mediated gene silencing vector derived from Cotton Leaf Crumple Virus (CLCrV). Transformed cotton plants showed greater chitinase activity than control, and they were resistant against nymphs and adults of A. gossypii. About 38.75% and 21.67% mortality of both nymphs and adults, respectively, were observed by using Chit1 of T. longibrachiatum. It is concluded that T. longibrachiatum showed promising results in controlling aphids by producing fungal chitinase in cotton plants and could be used as an effective method in the future.

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“…Chitinases (EC 3.2.1.14) are hydrolytic enzymes that cleave glycosidic linkages in chitin. As a result, chitinases have molecular weights ranging from 20 to 90 kDa [10]. Chitinases can break down chitin directly into low molecular weight chitooligomers, which have a variety of commercial, agricultural, and medical applications, including elicitor activity and anticancer potential [11,12].…”

Section: Introductionmentioning

confidence: 99%

Antioxidants, Antimicrobial, and Anticancer Activities of Purified Chitinase of Talaromyces funiculosus Strain CBS 129594 Biosynthesized Using Crustacean Bio-Wastes

et al. 2022

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Talaromyces funiculosus strain CBS 129594 was optimized to promote chitinase activity under solid state fermentation using crustacean bio-wastes. The aim of the study was to use purified chitinase as antioxidant, antimicrobial, and anticancer activities. The results showed that the maximum enzyme yield (2.98 ± 0.2 U/g substrate) was obtained at 1:2 crab shell chitin with the inoculation size (2.5 × 106 v/v) after seven days of incubation, pH 6.5, using 0.20% of soybean meal, malt extract, and yeast extract and 100% cane and beet molasses as supplementation. The enzyme was purified with an overall yield of 7.22 purification fold with a specific activity of 9.32 ± 0.3 U/mg protein. The molecular mass of the purified chitinase was 45 kDa. The highest chitinase activity was detected at pH 6.5 and 40 °C. The purified chitinase was activated by Ca2+, Cu2+, Na+, Mn2+, and Mg2+. On the other hand, the enzyme activity was inhibited in the presence of Hg2+, Ag2+, and Li+ at 10 mM, while Zn2+ and Co2+ caused no effect compared to media without any metals. The scavenging of 2.2-diphenyl-1-picrylhydrazyl (DPPH) radicals and 2.2-pheny-l-1-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) increased with increasing the concentrations of the purified chitinase enzyme (100, 200, 300, and 400 µg/mL) which ranged from 48.7% to 57.8% and 8.87% to 63.73%, respectively. The IC50 value of DPPH radicals and ABTS of purified chitinase produced by T. funiculosus strain CBS 129594 was 199 and 306 μg/mL concentration, respectively. The purified chitinase inhibited the growth of Gram-negative bacteria (Pseudomonas aeruginosa, Escherichia coli), Gram-positive bacteria (Bacillus subtilis, Staphylococcus aureus), and fungi (Aspergillus niger, Candida albicans). The highest concentrations of purified chitinase (1000 µg/mL) caused the higher toxicity of cancer cell line MCF7 (97%), HCT116 (88.2%), and HepG2 (97.1%). In conclusion, we can conclude that chitinase can be produced from marine waste and can be used as an antioxidant, antibacterial activity, cancer therapy, and ecofriendly biocontrol agent.

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Myco-chitinases as versatile biocatalysts for translation of coastal residual resources to eco-competent chito-bioactives

Cited by 6 publications

References 118 publications

Purification, Characterization and Antifungal Activity of the Aspergillus niveus Chitinase Produced Using Shrimp Shells

Purification, Characterization and Antifungal Activity of the Aspergillus niveus Chitinase Produced Using Shrimp Shells

Chitinase of Trichoderma longibrachiatum for control of Aphis gossypii in cotton plants

Antioxidants, Antimicrobial, and Anticancer Activities of Purified Chitinase of Talaromyces funiculosus Strain CBS 129594 Biosynthesized Using Crustacean Bio-Wastes

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