Mining of Novel Myrosinase with High Activity Based on Sequence and Structure Clustering for Efficient Preparation of Sulforaphane

Sulforaphane has garnered significant research attention owing to its potent and promising biological activities. Mining the highly active myrosinase is the key to preparing sulforaphane. In this study, a novel myrosinase, designated Semyr, was identified from <i>Serratia plymuthica</i> through sequence and structural clustering analysis. The enzyme was heterologously expressed in <i>Escherichia coli</i>, demonstrating a sinigrin hydrolysis activity of 110.48 U/mg, which constitutes the highest recombinant myrosinase activity reported to date. A reaction system was established to prepare sulforaphane. 60 U of myrosinase was added to 5 mL of substrate, yielding 15.39 mg of sulforaphane per gram of broccoli seeds after 20 min at 40 °C and pH 6.0, with a conversion rate of 96.50%. Concurrently, the highest productivity of 5.55 μmol/g·min for sulforaphane was achieved after 15 min. Thus, Semyr serves as a valuable biocatalytic tool for the efficient preparation of sulforaphane.

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Publication Details

Journal
Journal of Agricultural and Food Chemistry
Published
2025-03-13
DOI
https://doi.org/10.1021/acs.jafc.5c00978
Citations
4
Primary Topic
Genomics, phytochemicals, and oxidative stress
Type
article
Field-Weighted Citation Impact
3.22

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article

Mining of Novel Myrosinase with High Activity Based on Sequence and Structure Clustering for Efficient Preparation of Sulforaphane

Mohamed Abdel aziz Balah, Changhu Xue, Hamed I. Hamouda, Xiangzhao Mao et al.
4 citations
Journal of Agricultural and Food Chemistry
Genomics, phytochemicals, and oxidative stress
3.22
article

Mining of Novel Myrosinase with High Activity Based on Sequence and Structure Clustering for Efficient Preparation of Sulforaphane

Mohamed Abdel aziz Balah, Changhu Xue, Hamed I. Hamouda, Xiangzhao Mao, Hong Jiang, Suxue Chen, Jiaqi Wang, Zhe Wang, Yán Li
article en
4 citations

Abstract

Sulforaphane has garnered significant research attention owing to its potent and promising biological activities. Mining the highly active myrosinase is the key to preparing sulforaphane. In this study, a novel myrosinase, designated Semyr, was identified from <i>Serratia plymuthica</i> through sequence and structural clustering analysis. The enzyme was heterologously expressed in <i>Escherichia coli</i>, demonstrating a sinigrin hydrolysis activity of 110.48 U/mg, which constitutes the highest recombinant myrosinase activity reported to date. A reaction system was established to prepare sulforaphane. 60 U of myrosinase was added to 5 mL of substrate, yielding 15.39 mg of sulforaphane per gram of broccoli seeds after 20 min at 40 °C and pH 6.0, with a conversion rate of 96.50%. Concurrently, the highest productivity of 5.55 μmol/g·min for sulforaphane was achieved after 15 min. Thus, Semyr serves as a valuable biocatalytic tool for the efficient preparation of sulforaphane.

Journal of Agricultural and Food ChemistryVol. 73(13)
China Light Industry Press (China) (CN), Institute of Plant Protection (CN), Qingdao National Laboratory for Marine Science and Technology (CN), Desert Research Center (EG), Ocean University of China (CN), Egyptian Petroleum Research Institute (EG)
National Natural Science Foundation of China, Natural Science Foundation of Hainan Province, Natural Science Foundation of Shandong Province, Taishan Scholar Project of Shandong Province, Fundamental Research Funds for the Central Universities
Openalex Percentile: Top 9%
Genomics, phytochemicals, and oxidative stress
3.22
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