Structure, degree of polymerization, and starch hydrolase inhibition activities of bird cherry (Prunus padus) proanthocyanidins

Yan Zhang; Dalong Li; Jinli Qiao; Yana Ni; Pei Liu; Dejian Huang; Junwei Huo

doi:10.1016/j.foodchem.2022.132588

Structure, degree of polymerization, and starch hydrolase inhibition activities of bird cherry (Prunus padus) proanthocyanidins

Food Chem. 2022 Aug 15:385:132588. doi: 10.1016/j.foodchem.2022.132588. Epub 2022 Feb 26.

Authors

Yan Zhang¹, Dalong Li², Jinli Qiao³, Yana Ni³, Pei Liu³, Dejian Huang⁴, Junwei Huo⁵

Affiliations

¹ Key Laboratory of Biology and Genetic Improvement of Horticultural Crops (Northeast Region), Ministry of Agriculture and Rural Affairs, Northeast Agricultural University, Harbin 150030, China; National-Local Joint Engineering Research Center for Development and Utilization of Small Fruits in Cold Regions, Northeast Agricultural University, Harbin 150030, China; College of Horticulture and Landscape Architecture, Northeast Agricultural University, Harbin 150030, China. Electronic address: zhang_yan@neau.edu.cn.
² Key Laboratory of Biology and Genetic Improvement of Horticultural Crops (Northeast Region), Ministry of Agriculture and Rural Affairs, Northeast Agricultural University, Harbin 150030, China; College of Horticulture and Landscape Architecture, Northeast Agricultural University, Harbin 150030, China.
³ National-Local Joint Engineering Research Center for Development and Utilization of Small Fruits in Cold Regions, Northeast Agricultural University, Harbin 150030, China; College of Horticulture and Landscape Architecture, Northeast Agricultural University, Harbin 150030, China.
⁴ Department of Food Science and Technology, National University of Singapore, 117543, Singapore.
⁵ Key Laboratory of Biology and Genetic Improvement of Horticultural Crops (Northeast Region), Ministry of Agriculture and Rural Affairs, Northeast Agricultural University, Harbin 150030, China; National-Local Joint Engineering Research Center for Development and Utilization of Small Fruits in Cold Regions, Northeast Agricultural University, Harbin 150030, China; College of Horticulture and Landscape Architecture, Northeast Agricultural University, Harbin 150030, China. Electronic address: huojunwei@neau.edu.cn.

PMID: 35303652
DOI: 10.1016/j.foodchem.2022.132588

Abstract

The structure of proanthocyanidins extracted from bird cherry fruits was characterized by HPLC-ESI/MS² and MALDI-TOF/MS analyses, and their subunits and mean degree of polymerization (mDP) were investigated by thiolysis reaction, and the inhibition activity against starch hydrolases measured using the high-throughput turbidity assay. This is the first mass spectrometric analysis to thoroughly investigate the structure and mDP of proanthocyanidins in bird cherry fruits. Bird cherry proanthocyanidins were categorized as oligomeric proanthocyanidins (mDP = 5.6), which constituted of (epi)gallocatechins and (epi)catechins. The proanthocyanidins increased from a (epi)gallocatechin-[(epi)catechin]₃ tetramer to a (epi)gallocatechin-[(epi)catechin]₁₁ dodecamer through the addition of one (epi)catechin with both A-type and B-type linkages. The proanthocyanidins had potent α-amylase and α-glucosidase inhibition activities with IC₅₀ values of 0.19 ± 0.01 µg/mL and 0.18 ± 0.006 µg/mL, comparing favorably to commercial drug acarbose. Bird cherry oligomeric proanthocyanidins are a promising starch hydrolase inhibitor for the application of potential functional food components.

Keywords: Bird cherry fruits; Inhibition activities; Proanthocyanidins; Starch hydrolases; Structure.

MeSH terms

Catechin* / chemistry
Polymerization
Proanthocyanidins* / analysis
Prunus*
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Starch
alpha-Amylases

Substances

Proanthocyanidins
Catechin
Starch
alpha-Amylases