FOOD SCIENCE ›› 2022, Vol. 43 ›› Issue (20): 53-62.doi: 10.7506/spkx1002-6630-20210907-089

• Food Chemistry • Previous Articles     Next Articles

Preparation and Structural Characterization of Mung Bean RS4·Se (IV) and Kinetics of Enzymatic Inhibition by It

ZHAO Shuting, WANG Weihao, QUAN Zhigang, WANG Juan, LIU Dezhi, WANG Yifei, WU Yunjiao, SU Youtao, WEI Chunhong, CAO Longkui   

  1. (1. College of Food Science, Heilongjiang Bayi Agricultural University, Daqing 163319, China; 2. National Coarse Cereals Engineering Research Center, Daqing 163319, China; 3. Heilongjiang Province Natural Products Simulated Moving Bed Chromatographic Separation Technology Innovation Center, Daqing 163319, China)
  • Online:2022-10-25 Published:2022-10-26

Abstract: In this paper, selenized mung bean resistant starch (MB-RS4?Se (IV)) was prepared from mung bean resistant starch (MB-RS4) by the nitric acid-sodium selenite method. Scanning electron microscopy (SEM) revealed that the starch granules were completely collapsed and fragmented after selenization. The structural characteristics of MB-RS4 and MB-RS4?Se (IV) were analyzed by ultraviolet (UV) spectroscopy, Fourier transform infrared (FTIR) spectroscopy, X-ray diffraction (XRD), gel permeation chromatography (GPC), and nuclear magnetic resonance (NMR). The results showed that selenization resulted in a red shift of the UV peak and a hyperchromic effect. Additionally, the characteristic peaks of Se=O, C–C (Se)2 and Se–O–C appeared at wavenumbers of 787.88, 730.88 and 654.75 cm-1, respectively, and the crystal structure was destroyed. The molecular mass dropped significantly, and MB-RS4·Se (IV)’s configuration was reversed and the C6 position was substituted compared with MB-RS4. MB-RS4·Se (IV) had a significantly enhanced inhibitory effect on α-glucosidase and α-amylase. The results of the enzymatic reaction kinetics showed that the inhibition of α-glucosidase was competitive type, and the inhibition of α-amylase was mixed anticompetitive type.

Key words: mung bean starch; selenization; structural properties; α-glucosidase; α-amylase; inhibition kinetics

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