Characterization of a novel sucrose phosphorylase from Paenibacillus elgii and its use in biosynthesis of α-arbutin

Characterization of a novel sucrose phosphorylase from Paenibacillus elgii and its use in biosynthesis of α-arbutin

α-Arbutin, a naturally occurring glycosylated derivative of hydroquinone (HQ), effectively inhibits melanin biosynthesis in epidermal cells. It is widely recognized as a fourth-generation whitening agent within the cosmetic industry. Currently, enzymatic catalysis is universally deemed the safest an...

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Bibliographic Details
Published in:World journal of microbiology & biotechnology Vol. 40; no. 1; p. 24
Main Authors: Su, Ruiyang, Zheng, Wan, Li, Anqi, Wu, Huawei, He, Yamei, Tao, Huimei, Zhang, Wangpu, Zheng, Hairui, Zhao, Zhenjun, Li, Shaobin
Format: Journal Article
Language:English
Published: Dordrecht Springer Netherlands 01-01-2024
Springer Nature B.V
Subjects:
Amino acid sequence
Applied Microbiology
Arbutin - metabolism
Biochemistry
Biomedical and Life Sciences
Biosynthesis
Biotechnology
Catalysis
E coli
Environmental Engineering/Biotechnology
Escherichia coli - genetics
Escherichia coli - metabolism
Hydroquinone
Hydroquinones - metabolism
Life Sciences
Melanin
Metal concentrations
Metal ions
Microbiology
Paenibacillus
Parameter sensitivity
pH effects
Phosphorylase
Phosphorylases
Sucrose
Sucrose phosphorylase
Sucrose phosphorylase
α-arbutin
Molecular chaperone
Paenibacillus elgii
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Summary:α-Arbutin, a naturally occurring glycosylated derivative of hydroquinone (HQ), effectively inhibits melanin biosynthesis in epidermal cells. It is widely recognized as a fourth-generation whitening agent within the cosmetic industry. Currently, enzymatic catalysis is universally deemed the safest and most efficient method for α-arbutin synthesis. Sucrose phosphorylase (SPase), one of the most frequently employed glycosyltransferases, has been extensively reported for α-arbutin synthesis. In this study, a previously reported SPase known for its effectiveness in synthesizing α-arbutin, was used as a probe sequence to identify a novel SPase from Paenibacillus elgii ( Pe SP) in the protein database. The sequence similarity between Pe SP and the probe was 39.71%, indicating a degree of novelty. Subsequently, the gene encoding Pe SP was coexpressed with the molecular chaperone pG-Tf2 in Escherichia coli , significantly improving Pe SP’s solubility. Following this, Pe SP was characterized and employed for α-arbutin biosynthesis. The specific activity of co-expressed Pe SP reached 169.72 U/mg, exhibited optimal activity at 35℃ and pH 7.0, with a half-life of 3.6 h under the condition of 35℃. Pe SP demonstrated excellent stability at pH 6.5–8.5 and sensitivity to high concentrations of metal ions. The kinetic parameters K m and k cat / K m were determined to be 14.50 mM and 9.79 min − 1 ·mM − 1 , respectively. The reaction conditions for α-arbutin biosynthesis using recombinant Pe SP were optimized, resulting in a maximum α-arbutin concentration of 52.60 g/L and a HQ conversion rate of 60.9%. The optimal conditions were achieved at 30℃ and pH 7.0 with 200 U/mL of Pe SP, and by combining sucrose and hydroquinone at a molar ratio of 5:1 for a duration of 25 h.
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ISSN:0959-3993
1573-0972
DOI:10.1007/s11274-023-03853-4