Characteristics of an β‐N‐Acetylhexosaminidase from <i>Bacillus</i> sp. CH11, Including its Transglycosylation Activity

Kurakake, Masahiro; Amai, Yukari; Konishi, Mizuki; Ikehira, Kaho

doi:10.1111/1750-3841.14125

Cited by 5 publications

(5 citation statements)

References 14 publications

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“…A change in optimal pH was also reported for the transglycosylation catalyzed by β‐ N ‐acetylhexosaminidase Bacillus sp. CH11 (Kurakake et al., 2018).…”

Section: Results and Disccusionmentioning

confidence: 99%

“…After centrifugation through a 0.22‐µm membrane filter at 10,000 × g for 5 min, the filtrate was analyzed by high‐performance liquid chromatography (HPLC). The transfer ratio [ G 3/( G 3 + ( G 1 – G 3)/2) × 100(%)] was calculated from the concentrations (M) of N ‐acetylglucosamine ( G 1) and N , N′ , N″ ‐triacetylchitotriose ( G 3) in the transfer product (Kurakake et al., 2018).…”

Section: Methodsmentioning

confidence: 99%

“…Bacillus sp. CH11 enzymes show high transglycosylation activity toward sugar alcohols as shown by the synthesis of 1‐O‐β‐ d ‐ N ‐acetylglucosaminyl xylitol using xylitol as an acceptor (Kurakake et al., 2018).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of a β‐N‐acetylhexosaminidase with transglycosylation activity from Metarhizium sp. A34

Kurakake

Amai

2022

Journal of Food Science

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In applications of chitin, one of the most abundant resources on earth, human milk oligosaccharides with many health functions were synthesized by transglycosylation of β‐N‐acetylhexosaminidase. Synthesis of new transfer products can be expected by other β‐N‐acetylhexosaminidases in nature. A total of 38 microorganisms that secrete β‐N‐acetylhexosaminidases with transglycosylation activity were isolated from a soil screen. Using N,N′‐diacetylchitobiose as the substrate, the transfer ratio increased with a decrease in substrate degradation when it was less than 60%. Metarhizium sp. A34 β‐N‐acetylhexosaminidase had high transglycosylation activity and showed a maximum production of the oligosaccharides against the substrate degradation where (GlcNAc)5 and (GlcNAc)4 were produced in addition to (GlcNAc)3. The maximum curve was attributed to a sequential reaction of transglycosylation followed by hydrolysis where oligosaccharides are an intermediate product and are hydrolyzed in a second step. The purified β‐N‐acetylhexosaminidase from Metarhizium sp. A34 had an optimal pH of 5 and was stable from pH 7 to 8. At pH 5, it had an optimal temperature of 40°C and was stable up to 30°C for 30 min. This enzyme had high thermostability up to 55°C when bound to the cell wall. The acceptor specificity for the transglycosylation reaction was enhanced for lower molecular weight sugar alcohols in the order of glycerin (C3), erythritol (C4), and xylitol (C5). The transfer product with glycerin was identified as 1‐O‐β‐d‐N‐acetylglucosaminyl glycerin, which may prove useful as a starting material for new glycolipids in food applications. Practical Application Metarhizium sp. A34 β‐N‐acetylhexosaminidase produced 1‐O‐β‐d‐N‐acetylglucosaminyl glycerin through the transglycosylation. Chitin oligosaccharides of the donor are obtained by hydrolysis of chitin. 1‐O‐β‐d‐N‐Acetylglucosaminyl glycerin may be useful to start material for the synthesis of new glycolipids. High thermostability of this enzyme is useful to prevention of contamination in the transglycosylation reaction.

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“…A change in optimal pH was also reported for the transglycosylation catalyzed by β‐ N ‐acetylhexosaminidase Bacillus sp. CH11 (Kurakake et al., 2018).…”

Section: Results and Disccusionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Characterization of a β‐N‐acetylhexosaminidase with transglycosylation activity from Metarhizium sp. A34

Kurakake

Amai

2022

Journal of Food Science

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“…These findings demonstrated that the two endo-1,3-β-glucanases from mollusks exhibit different transglycosylation specificities, although they share a high sequence identity. The unique transglycosylation activity of L cf towards sorbitol facilitates the development of glycoconjugates with intestinal functions, and noncariogenic sugars [ 35 ]. In sum, this study provided insights into novel endo-1,3-β-glucanases from marine mollusks, enhancing our understanding of the diverse enzymatic specificities of marine mollusk endo-1,3-β-glucanases.…”

Section: Resultsmentioning

confidence: 99%

Biochemical Characterization of a Novel Endo-1,3-β-Glucanase from the Scallop Chlamys farreri

Liu

Lyu

2020

Marine Drugs

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Endo-1,3-β-glucanases derived from marine mollusks have attracted much attention in recent years because of their unique transglycosylation activity. In this study, a novel endo-1,3-β-glucanase from the scallop Chlamys farreri, named Lcf, was biochemically characterized. Unlike in earlier studies on marine mollusk endo-1,3-β-glucanases, Lcf was expressed in vitro first. Enzymatic analysis demonstrated that Lcf preferred to hydrolyze laminarihexaose than to hydrolyze laminarin. Furthermore, Lcf was capable of catalyzing transglycosylation reactions with different kinds of glycosyl acceptors. More interestingly, the transglycosylation specificity of Lcf was different from that of other marine mollusk endo-1,3-β-glucanases, although they share a high sequence identity. This study enhanced our understanding of the diverse enzymatic specificities of marine mollusk endo-1,3-β-glucanases, which facilitated development of a unique endo-1,3-β-glucanase tool in the synthesis of novel glycosides.

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“…H11 25 , the β-glucosidases CelB from Pyrococcus furiosus 26 and SSG from Sulfolobus shibatae 27 , the β-galactosidases Bgal from Kluyveromyces lactis 28 and LacA from Aspergillus oryzae 29 , or the β-N-acetylhexosaminidase from Bacillus sp. CH11 30 . However, to the best of our knowledge, there are no known β-fructofuranosidases described to generate such compounds other than that from Arthrobacter sp.…”

Section: Introductionmentioning

confidence: 99%

New insights into the molecular mechanism behind mannitol and erythritol fructosylation by β-fructofuranosidase from Schwanniomyces occidentalis

Rodrigo-Frutos

Jiménez-Ortega

Piedrabuena

et al. 2020

Preprint

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The β-fructofuranosidase from Schwanniomyces occidentalis (Ffase) is a useful biotechnological tool for the fructosylation of different acceptors to produce fructooligosaccharides (FOS) and fructo-conjugates. In this work, the structural determinants of Ffase involved in the transfructosylating reaction of the alditols mannitol and erythritol have been studied in detail. Complexes with fructosyl-erythritol or sucrose were analyzed by crystallography and the effect of mutational changes in positions Gln-176, Gln-228, and Asn-254 revised to explore their role in modulating this biocatalytic process. Interestingly, N254T variant enhanced the wild-type protein production of fructosyl-erythritol and FOS by `30% and 48%, respectively. Moreover, it showed a shift towards neokestose, which represented ~27% of total FOS, and yielded 31.8 g l-1 blastose by using glucose as exclusive fructosyl-acceptor. Noteworthy, N254D and Q176E replacements turned the specificity of Ffase transferase activity towards the synthesis of the fructosylated polyols at the expense of FOS production, but without increasing the total reaction efficiency. The results presented here highlight the relevance of the pair Gln-228/Asn-254 for Ffase donor-sucrose binding and opens new windows of opportunity for optimizing the generation of fructosyl-derivatives by this enzyme enhancing its biotechnological applicability.

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Characteristics of an β‐N‐Acetylhexosaminidase from Bacillus sp. CH11, Including its Transglycosylation Activity

Cited by 5 publications

References 14 publications

Characterization of a β‐N‐acetylhexosaminidase with transglycosylation activity from Metarhizium sp. A34

Characterization of a β‐N‐acetylhexosaminidase with transglycosylation activity from Metarhizium sp. A34

Biochemical Characterization of a Novel Endo-1,3-β-Glucanase from the Scallop Chlamys farreri

New insights into the molecular mechanism behind mannitol and erythritol fructosylation by β-fructofuranosidase from Schwanniomyces occidentalis

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