Physicochemical Properties of Pectin Modified by Cross-Linking with Ferulic Acid under the Catalysis of Horseradish Peroxidase

doi:10.7506/spkx1002-6630-20190729-399

FOOD SCIENCE ›› 2020, Vol. 41 ›› Issue (14): 9-14.doi: 10.7506/spkx1002-6630-20190729-399

• Food Chemistry • Previous Articles Next Articles

Physicochemical Properties of Pectin Modified by Cross-Linking with Ferulic Acid under the Catalysis of Horseradish Peroxidase

LIU Yanzhao, LI Xiang, LIU Gongji, LI Jie, YAN Shoulei

(1. College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China;2. Aquatic Vegetables Preservation and Processing Technology Engineering Center of Hubei Province, Wuhan 430070, China)

Published:2020-07-29

Abstract

Abstract: In this study, in order to improve its functional properties and more broadly to enlarge its application scope, pectin from white radish was prepared by suction filtration followed by rotary evaporation and modified with ferulic acid as a cross-linker under the catalysis of horseradish peroxidase. The native and modified pectin were characterized by colorimeter, rheometer, scanning electron microscope and Fourier transform infrared spectroscopy. The results showed that after ferulic acid treatment, the pectin turned yellow, and its antioxidant potential significantly increased. In addition, ferulic acid treatment changed the surface microstructure, and cross-linked the dispersed pectin molecules together. The results of Fourier transform infrared spectroscopy and ultraviolet-visible spectroscopy indicated that ferulic acid and pectin combined together to form a new substance.

Key words: ferulic acid; radish pectin; horseradish peroxidase; modification

CLC Number:

TS254.58

LIU Yanzhao, LI Xiang, LIU Gongji, LI Jie, YAN Shoulei. Physicochemical Properties of Pectin Modified by Cross-Linking with Ferulic Acid under the Catalysis of Horseradish Peroxidase[J]. FOOD SCIENCE, 2020, 41(14): 9-14.

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Physicochemical Properties of Pectin Modified by Cross-Linking with Ferulic Acid under the Catalysis of Horseradish Peroxidase

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