FOOD SCIENCE ›› 2014, Vol. 35 ›› Issue (1): 1-6.doi: 10.7506/spkx1002-6630-201401001

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Characteristics of Bovine Serum Albumin-Anthocyanin Bioactive Nanoparticles

YAO Hui-fang, DONG Xue-yan, JING Hao*   

  1. Beijing Key Laboratory of Functional Food from Plant Resources, College of Food Science and Nutritional Engineering,
    China Agricultural University, Beijing 100083, China
  • Received:2013-01-24 Revised:2013-12-23 Online:2014-01-15 Published:2014-01-22
  • Contact: 景浩 JING Hao E-mail:hao.haojing@gmail.com

Abstract:

The nanoparticle formation between bovine serum albumin (BSA) and anthocyanin (ACN) was characterized
using scanning transmission electron microscope (STEM) and nanoparticles size analyzer. The anthocyanin-binding capacity
of BSA was studied by ammonium sulfate salting-out method. DPPH and ABTS radical scavenging capacities and release
characteristics in both simulated intestinal fluid (SIF) and simulated gastric fluid (SGF) systems were investigated for
oxidation stability of BSA-bound anthocyanin system. The results showed that both BSA and anthocyanin-bound BSA could
be self-assemble and form nanoparticles in phosphate buffer (pH 7.4), and the particle size (15–20 nm) of the anthocyaninbound
BSA was smaller than that of the BSA (30–35 nm). The molar binding ratio between BSA and antocyanin was 1:10.
The DPPH radical and ABTS+· scavenging abilities of BSA-bound anthocyanin were significantly stronger than those
of unbound anthocyanin. There was no significant difference in stability between unbound anthocyanin and BSA-bound
anthocyanin in SGF system, while significant difference in SIF system was observed. The content of unbound anthocyanin
decreased by approximately 70% after 6 hours; however, no significant change was observed for BSA-bound anthocyanin.
BSA revealed remarkable stabilizing effect on anthocyanin oxidation.

Key words: bovine serum albumin, anthocyanin, nanoparticles, binding capacity, oxidation stability

CLC Number: