Dataset Information

Identification and Characterization of a-Glucosidase Inhibition Flavonol Glycosides from Jack Bean (Canavalia ensiformis (L.) DC.

ABSTRACT: Although the intake of jack bean (Canavalia ensiformis (L.) DC.), an underutilized tropical legume, can potentially decrease the risk of several chronic diseases, not much effort has been directed at profiling the polyphenolics contained therein. Hence, this work aimed to identify and quantify the dominant jack bean polyphenolics, which are believed to have antioxidant and other bioactivities. Four major compounds were detected and identified as kaempferol glycosides with three or four glycoside units. Their structures were established based on UV-visible, 1d, 2D NMR, and HR-ESI-MS analyses. Specifically, kaempferol 3-O-a-l-rhamnopyranosyl (1®6)- b-d-glucopyranosyl (1®2)-b-d-galactopyranosyl-7-O-[3-O-o-anisoyl]-a-l-rhamnopyranoside was detected for the first time, while the other three compounds have already been described in plants other than jack bean. This new compound was found to have a higher a-glucosidase inhibition activity compared to acarbose.

SUBMITTER: Sutedja AM

PROVIDER: S-EPMC7321285 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature

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Publications

Identification and Characterization of a-Glucosidase Inhibition Flavonol Glycosides from Jack Bean (<i>Canavalia ensiformis</i> (L.) DC.

Sutedja Anita M AM Yanase Emiko E Batubara Irmanida I Fardiaz Dedi D Lioe Hanifah N HN

Molecules (Basel, Switzerland) 20200527 11

Although the intake of jack bean (<i>Canavalia ensiformis</i> (L.) DC.), an underutilized tropical legume, can potentially decrease the risk of several chronic diseases, not much effort has been directed at profiling the polyphenolics contained therein. Hence, this work aimed to identify and quantify the dominant jack bean polyphenolics, which are believed to have antioxidant and other bioactivities. Four major compounds were detected and identified as kaempferol glycosides with three or four gl ...[more]

PMID: 32471071

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Project description:Serine proteases has been vastly reported to be found (and identified) only in seed extracts of Canavalia ensiformis (C. ensiformis), however, our group observed expressive serine protease activities in aqueous extracts from leaves, seeds, roots, and stem, especially in a leaf extract obtained with distillated water (CE-A). Additionally, this extract demonstrated very good stability in high temperatures and in the presence of chemical agents. In order to study the serine protease activity in leaves, CE-A was submitted to benzamidine-sepharose affinity column and an enriched fraction of serine proteases, named CE-ABza was purified 1.65 fold, yielding a total recovery of about 62%. Based upon zymographic analysis in a gelatin-SDS-PAGE-, the CE-ABza fraction presented an enzymatic activity band at approximately 90 kDa molecular mass region under non-reducing conditions and three bands at 17, 32 and also at 90 kDa under reducing condition. This fraction was able to hydrolyze, in a different way, peptidomimetic and protein substrates. The maximal activity was observed at basic pH values (8.0 to 9.5) and temperature about 40°C. These enzymes exhibited important thermal stability and were significantly inhibited by serine protease inhibitors, such as benzamidine and TPCK. Calcium, magnesium, manganese and zinc ions had a negative modulation on the CE-ABza activity. Mass spectrometry-based proteomics approach identified showed homology with 11 plant proteases from different legumes species, indicating their presence or demonstrating that CE-Bza proteases share specific region of the primary structure of theses enzyme, although the C. ensiformis genome and protein databases are yet to be publicly available. These results demonstrated that these molecules found in both the CE-A extract and the CE-ABza fraction presented important properties that could be used as potential pharmacological and biotechnological targets as therapeutic option. Besides, identification and characterization of C. ensiformis proteases contribute to the studies of plant enzymes.

Dataset Information

Identification and Characterization of a-Glucosidase Inhibition Flavonol Glycosides from Jack Bean (Canavalia ensiformis (L.) DC.

Publications

Identification and Characterization of a-Glucosidase Inhibition Flavonol Glycosides from Jack Bean (<i>Canavalia ensiformis</i> (L.) DC.

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