Purification and characterization of an extracellular thermo-alkali stable, metal tolerant chitinase from Streptomyces chilikensis RC1830 isolated from a brackish water lake sediment

Ray, L. Bryan; Panda, Ananta Narayan; Mishra, Samir R.; Pattanaik, Ajit Kumar; Adhya, T. K.; Suar, Mrutyunjay; Raina, Vishakha

doi:10.1016/j.btre.2019.e00311

Cited by 25 publications

(31 citation statements)

References 11 publications

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“…Chitosan and CMC were resistant substrates for chitinase PbChi67, similar to the enzyme analysed by Fu et al (2016). On the other hand, chitinase Streptomyces chilikensis RC1830 demonstrated broad substrate-specificity, besides colloidal chitin effectively hydrolysing also xylan, CMC, starch and pectin (Ray et al 2019).…”

Section: Discussionsupporting

confidence: 64%

Purification, characterization and cloning of a chitinase from Stenotrophomonas rhizophila G22

et al. 2019

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In the presented research the extracellular chitinase of Stenotrophomonas rhizophila G22 was biochemically and molecularly characterized. The studied enzyme was purified from a 72-h bacterial culture about 14 times, with a recovery of 63%. The molecular weight of the purified protein was estimated at 50 kDa by SDS-PAGE. The enzyme showed high activity against colloidal chitin. Significantly lower activities were observed with native chitin powder and chitosan. Adsorption of the enzyme to colloidal chitin and to powdered chitin at the level of 75% and 37%, respectively, was observed after 30 min of reaction. Optimum temperature and pH were 37 °C and 5.9, respectively. The enzyme demonstrated higher activity against nitrophenyl-β d N, N′, N″-triacetylchitotriose and approx. 5 times lower activity for 4-nitrophenyl-N, N′-diacetylβ-d-chitobiose. The enzyme is an endochitinase, which is confirmed by the K m and V max values determined in the studies. S. rhizophila G22 endochitinase was inhibited in the presence of cysteine-specific inhibitors, which indicates the role of cysteine moieties in the mechanism of catalysis or in stabilisation of the enzyme molecule. Also Ca 2+ and Mn 2+ ions may stabilise the protein's spatial structure. SDS and ions: Fe 2+ , Cu 2+ , Co 2+ , Zn 2+ inhibited the activity of enzyme. A full-length (2109 bp) gene coding chitinase from S. rhizophila G22 was obtained. Four domains typical for glycoside hydrolase family 18 (GH 18) chitinases were identified: catalytic Gly_18, chitin-binding-ChtBD3, type-III fibronectin-FN3 and polycystic kidney disease domain-PKD domain.

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Section: Discussionsupporting

confidence: 64%

Purification, characterization and cloning of a chitinase from Stenotrophomonas rhizophila G22

et al. 2019

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“…The recombinant enzyme was then utilized for COS and GlcNAc production using CC and CHS as the substrates and observed to produce (GlcNAc) 1−2 and GlcNAc as the major products (Kidibule et al, 2018). Thermo-alkali stable, extracellular chitinase (10.5 kDa) was purified from Streptomyces chilikensis RC1830 isolated from brackish lake water sediment (Ray et al, 2019). The study suggested that purified enzymes possess a high binding affinity with CC as compared to starch, xylan, and carboxymethyl cellulose and have a significant conversion efficiency at 60 • C (pH 11).…”

Section: Enzymatic Approachmentioning

confidence: 99%

“…Thermo-alkali stable, extracellular chitinase (10.5 kDa) was purified from Streptomyces chilikensis RC1830 isolated from brackish lake water sediment (Ray et al, 2019 ). The study suggested that purified enzymes possess a high binding affinity with CC as compared to starch, xylan, and carboxymethyl cellulose and have a significant conversion efficiency at 60°C (pH 11).…”

Section: Strategies For Cos and Glcnac Productionmentioning

confidence: 99%

Chemoenzymatic Production and Engineering of Chitooligosaccharides and N-acetyl Glucosamine for Refining Biological Activities

et al. 2020

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Chitooligosaccharides (COS) and N-acetyl glucosamine (GlcNAc) are currently of enormous relevance to pharmaceutical, nutraceutical, cosmetics, food, and agriculture industries due to their wide range of biological activities, which include antimicrobial, antitumor, antioxidant, anticoagulant, wound healing, immunoregulatory, and hypocholesterolemic effects. A range of methods have been developed for the synthesis of COS with a specific degree of polymerization along with high production titres. In this respect, chemical, enzymatic, and microbial means, along with modern genetic manipulation techniques, have been extensively explored; however no method has been able to competently produce defined COS and GlcNAc in a mono-system approach. Henceforth, the chitin research has turned toward increased exploration of chemoenzymatic processes for COS and GlcNAc generation. Recent developments in the area of green chemicals, mainly ionic liquids, proved vital for the specified COS and GlcNAc synthesis with better yield and purity. Moreover, engineering of COS and GlcNAc to generate novel derivatives viz. carboxylated, sulfated, phenolic acid conjugated, amino derived COS, etc., further improved their biological activities. Consequently, chemoenzymatic synthesis and engineering of COS and GlcNAc emerged as a useful approach to lead the biologically-active compound-based biomedical research to an advanced prospect in the forthcoming era.

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“…O-7 29 . Also, the Streptomyces chilikensis RC1830 produced chitinase was active between pH 5-8 with an optimum pH 7 37 . The activity of chitinase produced from certain marine bacterias like Sphingomonas sp.…”

Section: Effect Of Temperature and Ph On The Stability And Activity Omentioning

confidence: 99%

Bioconversion of chitin and concomitant production of chitinase and N-acetylglucosamine by novel Achromobacter xylosoxidans isolated from shrimp waste disposal area

Shanmugam

Sadaiappan

Aruni

et al. 2020

Sci Rep

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Marine pollution is a significant issue in recent decades, with the increase in industries and their waste harming the environment and ecosystems. Notably, the rise in shellfish industries contributes to tons of shellfish waste composed of up to 58% chitin. Chitin, the second most ample polymer next to cellulose, is insoluble and resistant to degradation. It requires chemical-based treatment or enzymatic hydrolysis to cleave the chitin polymers. the chemical-based treatment can lead to environmental pollution, so to solve this problem, enzymatic hydrolysis is the best option. Moreover, the resulting biopolymer by-products can be used to boost the fish immune system and also as drug delivery agents. Many marine microbial strains have chitinase producing ability. Nevertheless, we still lack an economical and highly stable chitinase enzyme for use in the industrial sector. So we isolate a novel marine bacterial strain Achromobacter xylosoxidans from the shrimp waste disposal site using chitin minimal medium. Placket-Burman and central composite design statistical models for culture condition optimisation predicted a 464.2 U/ml of chitinase production. The culture conditions were optimised for maximum chitinase production recording up to 467 U/ml. This chitinase from the A. xylosoxidans was 100% active at an optimum temperature of 45 °C (withstand up to 55 °C) and pH 8 with 80% stability. The HPLC analysis of chitinase degraded shellfish waste reveals a major amino acid profile composition-arginine, lysine, aspartic acid, alanine, threonine and low levels of isoleucine and

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Purification and characterization of an extracellular thermo-alkali stable, metal tolerant chitinase from Streptomyces chilikensis RC1830 isolated from a brackish water lake sediment

Abstract: Graphical abstract

Cited by 25 publications

References 11 publications

Purification, characterization and cloning of a chitinase from Stenotrophomonas rhizophila G22

Purification, characterization and cloning of a chitinase from Stenotrophomonas rhizophila G22

Chemoenzymatic Production and Engineering of Chitooligosaccharides and N-acetyl Glucosamine for Refining Biological Activities

Bioconversion of chitin and concomitant production of chitinase and N-acetylglucosamine by novel Achromobacter xylosoxidans isolated from shrimp waste disposal area

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