Efficient conversion of crystalline chitin to N-acetylglucosamine and N,N'-diacetylchitobiose by the enzyme cocktail produced by Paenibacillus sp. LS1

Mukherjee, Saumashish; Behera, Prashanta Kumar; Madhuprakash, Jogi

doi:10.1016/j.carbpol.2020.116889

Cited by 26 publications

(42 citation statements)

References 46 publications

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“…The enzyme cocktail of strain Paenibacillus sp. LS1 can produce GlcNAc and (GlcNAc) 2 with minor (GlcNAc) 3 from crystalline α-chitin [ 30 ]. The crude enzyme of Aeromonas hydrophila H-2330 mainly produces GlcNAc from crystalline α-chitin [ 31 ].…”

Section: Resultsmentioning

confidence: 99%

“…Because the natural source of chitin is crystalline chitin, chitinases that can efficiently hydrolyze crystalline chitin have better application potential in preparing COSs and GlcNAc from natural chitin sources than those only active on colloidal chitin. However, so far, only a few crude enzymes produced by wild strains and recombinant chitinases have been reported to be used in preparing COSs and GlcNAc from crystalline chitin [ 27 , 30 , 31 , 32 , 33 ]. Thus, it is necessary to identify and characterize more chitinases that can efficiently hydrolyze crystalline chitin for preparing COSs and GlcNAc from natural chitin sources.…”

Section: Introductionmentioning

confidence: 99%

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Identification and Characterization of Three Chitinases with Potential in Direct Conversion of Crystalline Chitin into N,N′-diacetylchitobiose

Ren

Dang

et al. 2022

Marine Drugs

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Chitooligosaccharides (COSs) have been widely used in agriculture, medicine, cosmetics, and foods, which are commonly prepared from chitin with chitinases. So far, while most COSs are prepared from colloidal chitin, chitinases used in preparing COSs directly from natural crystalline chitin are less reported. Here, we characterize three chitinases, which were identified from the marine bacterium Pseudoalteromonas flavipulchra DSM 14401T, with an ability to degrade crystalline chitin into (GlcNAc)2 (N,N’-diacetylchitobiose). Strain DSM 14401 can degrade the crystalline α-chitin in the medium to provide nutrients for growth. Genome and secretome analyses indicate that this strain secretes six chitinolytic enzymes, among which chitinases Chia4287, Chib0431, and Chib0434 have higher abundance than the others, suggesting their importance in crystalline α-chitin degradation. These three chitinases were heterologously expressed, purified, and characterized. They are all active on crystalline α-chitin, with temperature optima of 45–50 °C and pH optima of 7.0–7.5. They are all stable at 40 °C and in the pH range of 5.0–11.0. Moreover, they all have excellent salt tolerance, retaining more than 92% activity after incubation in 5 M NaCl for 10 h at 4 °C. When acting on crystalline α-chitin, the main products of the three chitinases are all (GlcNAc)2, which suggests that chitinases Chia4287, Chib0431, and Chib0434 likely have potential in direct conversion of crystalline chitin into (GlcNAc)2.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of Three Chitinases with Potential in Direct Conversion of Crystalline Chitin into N,N′-diacetylchitobiose

Ren

Dang

et al. 2022

Marine Drugs

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“…Despite the high production rates of chitin waste from different seafood industries [9], this compound does not accumulate in nature, as it can be hydrolysed by the chitinases secreted by chitinolytic micro-organisms. Therefore, microbe-mediated degradation could serve as a potential eco-friendly alternative for chitin depolymerization [10].…”

Section: Full-textmentioning

confidence: 99%

Identification of Mucilaginibacter conchicola sp. nov., Mucilaginibacter achroorhodeus sp. nov. and Mucilaginibacter pallidiroseus sp. nov. and emended description of the genus Mucilaginibacter

Kim

Lee

Chhetri

et al. 2022

International Journal of Systematic and Evolutionary Microbiology

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Three chitinolytic, Gram-negative, light pink, capsule-forming, rod-shaped bacterial strains with gliding motion (MYSH2T, MJ1aT and dk17T) were isolated from seashells, soil and foxtail, respectively. Phylogenetic analysis of the 16S rRNA gene sequences and concatenated alignment of 92 core genes indicated that strains MYSH2T, MJ1aT and dk17T were novel species of the genus Mucilaginibacter and exhibited a high 16S rRNA sequence similarity (i.e. more than 97.2 %) among each other. These novel strains contained summed feature 3 (C16:1 ω7c and/or C16:1 ω6), iso-C15:0 and MK-7 as the predominant fatty acids and menaquinone. According to the CAZys coding gene of KAAS, MYSH2T and MJ1aT were interpreted as strains containing both GH18 and 19 family coding genes, except for dk17T, which shows only GH19 family genes. These strains likely degrade chitin to chitobiose or directly to N-acetyl-d-glucosamine, which may enhance their chitinolytic capacity, thus making these stains potentially useful for industrial chitin degradation. Based on distinct morphological, physiological, chemotaxonomic and phylogenetic differences from their closest phylogenetic neighbours, we propose that strains MYSH2T, MJ1aT and dk17T represent three novel species in the genus Mucilaginibacter , for which the names Mucilaginibacter conchicola sp. nov. (=KACC 19716T=JCM 32787T), Mucilaginibacter achroorhodeus sp. nov. (=KACC 19906T=NBRC 113667T) and Mucilaginibacter pallidiroseus sp. nov. (=KACC 19907T=NBRC 113666T) are proposed. An emended description of the genus Mucilaginibacter is proposed.

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“…Due to its biodegradability, biocompatibility, antimicrobial activity, and non-toxicity, there is a strong growing commercial interest in chitin and chitin-based products, such as the watersoluble chitin variant chitosan, a heteropolymer of N-acetyl-glucosamine and glucosamine and chito-oligosaccharides. Major applications include use in medicine, agriculture and cosmetics (Madhuprakash et al, 2014(Madhuprakash et al, , 2015Liaqat and Eltem, 2018;Mukherjee et al, 2020;Rani et al, 2020aRani et al, , 2020b. Chitin and chitosan derivatives were also employed as biosorbents for removal of various metal ions, radionuclides, dyes and phenols from wastewaters due to the high proportion of amino and hydroxyl functional groups within the polymer chains (Bhatnagar and Sillanpää, 2009).…”

Section: Introductionmentioning

confidence: 99%

“…Owing to the several complications associated with chemical processes, enzymatic methods of chitin valorization are gaining importance for sustainable production of chitin and chitosan derivatives (Mukherjee et al, 2020;Rani et al, 2020aRani et al, , 2020bHarmsen et al, 2020). Bacteria, in nature degrade and/or modify chitin by employing an array of chitinolytic enzymes that act synergistically.…”

Section: Introductionmentioning

confidence: 99%

Genome analysis of Streptomyces sp. UH6 revealed the presence of potential chitinolytic machinery crucial for chitosan production

Duhsaki

Mukherjee

Rani

et al. 2021

Environ Microbiol Rep

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Summary Chitosan and its derivatives have numerous applications in wastewater treatment as bio‐coagulants, flocculants and bio‐adsorbents against both particulate and dissolved pollutants. Chitinolytic bacteria secrete an array of enzymes, which play crucial role in chitin to chitosan conversion. Consequently, there is a growing demand for identification and characterization of novel bacterial isolates with potential implications in chitosan production. We describe genomic features of the new isolate Streptomyces sp. UH6. Analysis of the 6.51 Mb genome revealed the GC content as 71.95% and presence of 6990 coding sequences of which 63% were functionally annotated. Further, we identified two possible chitin‐utilization pathways, which employ secreted enzymes like lytic polysaccharide monooxygenases and family‐18 glycoside hydrolases (GHs). More importantly, the genome has six family‐4 polysaccharide deacetylases with probable role in chitin to chitosan conversion, as well as two chitosanases belonging to GH46 and GH75 families. In addition, the gene clusters, dasABC and ngcEFG coding for transporters, which mediate the uptake of N,N′‐diacetylchitobiose and N‐acetyl‐d‐glucosamine were identified. Several genes responsible for hydrolysis of other polysaccharides and fermentation of sugars were also identified. Taken together, the phylogenetic and genomic analyses suggest that the isolate Streptomyces sp. UH6 secretes potential chitin‐active enzymes responsible for chitin to chitosan conversion.

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Efficient conversion of crystalline chitin to N-acetylglucosamine and N,N'-diacetylchitobiose by the enzyme cocktail produced by Paenibacillus sp. LS1

Cited by 26 publications

References 46 publications

Identification and Characterization of Three Chitinases with Potential in Direct Conversion of Crystalline Chitin into N,N′-diacetylchitobiose

Identification and Characterization of Three Chitinases with Potential in Direct Conversion of Crystalline Chitin into N,N′-diacetylchitobiose

Identification of Mucilaginibacter conchicola sp. nov., Mucilaginibacter achroorhodeus sp. nov. and Mucilaginibacter pallidiroseus sp. nov. and emended description of the genus Mucilaginibacter

Genome analysis of Streptomyces sp. UH6 revealed the presence of potential chitinolytic machinery crucial for chitosan production

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