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Separation, Purification, and Purity Identification of Cd-Binding Protein from Rice

CHEN Lu, , CAI Jun, DING Wenping, WU Yongning   

  1. 1. College of Food Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, China;
    2. Hubei Collaborative Innovation Center for Processing of Agricultural Products, Wuhan 430023, China;
    3. National Center for Food Safety Risk Assessment, Beijing 100021, China
  • Online:2016-07-15 Published:2016-07-26
  • Contact: CHEN Jiwang

Abstract:

A graphite furnace atomic absorption spectrometry (GFAAS) method was used to determine the cadmium content
in rice grains from different varieties and at milling levels, as well as in four rice seed storage proteins (albumin, globulin,
prolamin and glutelin) obtained through the Osborne sequential extraction method. Moreover, rice cadmium-binding protein
(RCBP) was separated and purified to homogeneity by using ultrafiltration and ion exchange chromatography. The purity and
molecular mass of RCBP were identified. The results showed that the cadmium content in indica rice was higher than that in
glutinous rice and japonica rice and the cadmium content in rice decreased with the increase of milling level. The cadmium
contents of rice albumin, globulin, prolamin, and glutelin were 0.66, 0.31, 0.63 and 0.23 μg/g, respectively. RCBP (fraction c)
with high purity and good homogeneity as well as molecular mass of 14 kD was prepared from rice albumin (RA).

Key words: rice Cd-binding protein, separation and purification, ion exchange chromatography, molecular mass

CLC Number: