A β-Primeverosidase-like Enzyme in Soybean [<i>Glycine max</i> (L.) Merr] Hypocotyls: Specificity toward 1-Octen-3-yl and 3-Octanyl β-Primeverosides-Reference-Cited by-同舟云学术

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A β-Primeverosidase-like Enzyme in Soybean [Glycine max (L.) Merr] Hypocotyls: Specificity toward 1-Octen-3-yl and 3-Octanyl β-Primeverosides

Published:2024-03-29 Issue:14 Volume:72 Page:8126-8139
ISSN:0021-8561
Container-title:Journal of Agricultural and Food Chemistry
language:en
Short-container-title:J. Agric. Food Chem.

Author:

Feng Xiaoxiao¹²,Zhu Yiwen¹,Cui Zhiyong¹,Li Xingfei²,Hua Yufei²^ORCID,Liu Yuan¹^ORCID

Affiliation:

1. Department of Food Science & Technology, School of Agriculture & Biology, Shanghai Jiao Tong University, Shanghai 200240, China

2. School of Food Science and Technology, State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China

Funder

China Postdoctoral Science Foundation

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.4c00436

Reference47 articles.

1. Volatile Glycosylation in Tea Plants: Sequential Glycosylations for the Biosynthesis of Aroma β-Primeverosides Are Catalyzed by Two Camellia sinensis Glycosyltransferases

2. Attractive but Toxic: Emerging Roles of Glycosidically Bound Volatiles and Glycosyltransferases Involved in Their Formation

3. Enzymatic Bioconversion of Cycloastragenol-6-O-β-D-glucoside into Cycloastragenol by a Novel Recombinant β-Glucosidase from Phycicoccus sp. Soil748

4. From Acetoin to (Z)-3-Hexen-1-ol: The Diversity of Volatile Organic Compounds that Induce Plant Responses

5. Functional characterizations of β-glucosidases involved in aroma compound formation in tea ( Camellia sinensis )

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