A Bacillus pumilus originated β-N-acetylglucosaminidase for chitin combinatory hydrolysis and exploration of its thermostable mechanism

Du, Chao; Jiang, Shun; Jiang, Sijing; Zhou, Yanmin; Zhang, Guimin

doi:10.1016/j.ijbiomac.2019.04.054

Cited by 18 publications

(17 citation statements)

References 42 publications

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“…Enzyme activity and stability, especially thermal and pH stability, must be considered in the industrial application. A few NAGases have good stability at 60 • C or above, such as BsNagZ (Jiang et al, 2019), BpNagZ from B. pumilus (Du et al, 2019), CbsA from Thermotoga neapolitana (Kim et al, 2015), and NahA from Symbiobacterium thermophilum (Ogawa et al, 2006; Table 3). In this research, the optimum reaction temperature and pH of BlNagZ was 60 • C and 5.5.…”

Section: Discussionmentioning

confidence: 99%

“…Then the mixture was filtered by 0.22 µm filter membrane after processed at 100 • C for 10 min. The end products were analyzed by HPLC (Du et al, 2019).…”

Section: Combinatory Hydrolysis Of Chitinmentioning

confidence: 99%

“…The enzymatic hydrolysis of chitin with mild reaction conditions, higher product purity and environmental friendliness becomes a great promising strategy for producing GlcNAc. The complete degradation of chitin to GlcNAc requires the synergistic action of chitinases and β-N-Acetylglucosaminidases (NAGases), that is, the colloidal chitin was hydrolyzed into chitin-oligosaccharides by chitinases, and further hydrolyzed into GlcNAc by NAGases (Du et al, 2019). Chitinase, such as ChiA, had achieved high-efficiency expression in our lab (Song et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

“…Several NAGases were already expressed inside the cells of E. coli, which required cell lysis during the purification (Zhou et al, 2016;Du et al, 2019). For ease of the process, BsNagZ secretory expression in Pichia pastoris with multiple copy strategy has been conducted, which takes 14 days per fermentation (Jiang et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

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High-Level Extracellular Expression of a New β-N-Acetylglucosaminidase in Escherichia coli for Producing GlcNAc

Jiang

et al. 2021

Front. Microbiol.

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N-acetyl-β-D glucosamine (GlcNAc) is wildly used in cosmetics, nutraceuticals and pharmaceuticals. The traditional chemical process for GlcNAc production from chitin causes serious acidic pollution. Therefore, the enzymatic hydrolysis becomes a great promising and alternative strategy to produce GlcNAc. β-N-acetylglucosaminidase (NAGase) can hydrolyze chitin to produce GlcNAc. Here, a GH3 family NAGase encoding gene BlNagZ from Bacillus licheniformis was expressed extracellularly in Escherichia coli guided by signal peptide PelB. The recombinant BlNagZ presented the best activity at 60°C and pH 5.5 with a high specific activity of 13.05 U/mg. The BlNagZ activity in the fermentation supernatant can reach 13.62 U/mL after optimizing the culture conditions, which is 4.25 times higher than optimization before. Finally, combining BlNagZ with chitinase ChiA we identified before, chitin conversion efficiency to GlcNAc can reach 89.2% within 3.5 h. In all, this study provided not only a high active NAGase, and a secreted expression strategy to reduce the cost of production, which is conducive to the industrial application.

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Section: Discussionmentioning

confidence: 99%

“…Then the mixture was filtered by 0.22 µm filter membrane after processed at 100 • C for 10 min. The end products were analyzed by HPLC (Du et al, 2019).…”

Section: Combinatory Hydrolysis Of Chitinmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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High-Level Extracellular Expression of a New β-N-Acetylglucosaminidase in Escherichia coli for Producing GlcNAc

Jiang

et al. 2021

Front. Microbiol.

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“…Chitooligosaccharides also function as biostimulators in plant growth and are used as biopesticides and biofertilizers in agriculture [29,30]. The application of chitinase and acetyl-glucosaminidases for industrial purposes has been reported [31][32][33]. Generally, chitooligosaccharides are obtained by chemical degradation or enzymatic hydrolysis [34,35].…”

Section: Introductionmentioning

confidence: 99%

Crab-Eating Monkey Acidic Chitinase (CHIA) Efficiently Degrades Chitin and Chitosan under Acidic and High-Temperature Conditions

et al. 2022

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Chitooligosaccharides, the degradation products of chitin and chitosan, possess anti-bacterial, anti-tumor, and anti-inflammatory activities. The enzymatic production of chitooligosaccharides may increase the interest in their potential biomedical or agricultural usability in terms of the safety and simplicity of the manufacturing process. Crab-eating monkey acidic chitinase (CHIA) is an enzyme with robust activity in various environments. Here, we report the efficient degradation of chitin and chitosan by monkey CHIA under acidic and high-temperature conditions. Monkey CHIA hydrolyzed α-chitin at 50 °C, producing N-acetyl-D-glucosamine (GlcNAc) dimers more efficiently than at 37 °C. Moreover, the degradation rate increased with a longer incubation time (up to 72 h) without the inactivation of the enzyme. Five substrates (α-chitin, colloidal chitin, P-chitin, block-type, and random-type chitosan substrates) were exposed to monkey CHIS at pH 2.0 or pH 5.0 at 50 °C. P-chitin and random-type chitosan appeared to be the best sources of GlcNAc dimers and broad-scale chitooligosaccharides, respectively. In addition, the pattern of the products from the block-type chitosan was different between pH conditions (pH 2.0 and pH 5.0). Thus, monkey CHIA can degrade chitin and chitosan efficiently without inactivation under high-temperature or low pH conditions. Our results show that certain chitooligosaccharides are enriched by using different substrates under different conditions. Therefore, the reaction conditions can be adjusted to obtain desired oligomers. Crab-eating monkey CHIA can potentially become an efficient tool in producing chitooligosaccharide sets for agricultural and biomedical purposes.

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Talaromyces pinophilus strain M13: a portrayal of novel groundbreaking fungal strain for phytointensification

Patel

Patel³

et al. 2020

Environ Sci Pollut Res

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A Bacillus pumilus originated β-N-acetylglucosaminidase for chitin combinatory hydrolysis and exploration of its thermostable mechanism

Cited by 18 publications

References 42 publications

High-Level Extracellular Expression of a New β-N-Acetylglucosaminidase in Escherichia coli for Producing GlcNAc

High-Level Extracellular Expression of a New β-N-Acetylglucosaminidase in Escherichia coli for Producing GlcNAc

Crab-Eating Monkey Acidic Chitinase (CHIA) Efficiently Degrades Chitin and Chitosan under Acidic and High-Temperature Conditions

Talaromyces pinophilus strain M13: a portrayal of novel groundbreaking fungal strain for phytointensification

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