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Purification and characterization of caclium-binding soybean protein
来源:Food Chem.141(2013)1645–1650
发布时间:2015-10-21 14:53:32
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Ying Lv a,b,1, Xiaolan Bao c,1, He Liu d,1, Jianhua Ren d, Shuntang Guo d,*

 


a. Beijing Key Laboratory of Agricultural Product Detection and Control of Spoilage Organisms and Pesticide Residue, Beijing 102206, China
b. College of Food Science and Engineering, Beijing University of Agriculture, Beijing 102206, China
c. Department of Food Science, Inner Mongolia Agricultural University, Huhehaote City 010018, China
d. College of Food Science & Nutritional Engineering, China Agricultural University, Beijing 100083, China

 

Abstract

Soybean protein hydrolysates (SPHs) can bind calcium in order to form soluble peptide-calcium com-plexes. However, amino acid composition and structural characteristics of the calcium chelating SPHs are still unclear. This study separated SPHs with calcium and iron immobilized metal affinity chromatog-raphy (IMAC), and examined the effects of SPHs with different amino acid composition on calcium bind-ing capacity. Three fractions (FFe-1,FFe-2 and FFe-3) isolated with IMAC-Fe3+ were shown possessing increased Glu, Gln, Lys and Pro content from FFe-1to FFe-3, and improved amount of bound calcium. Fur-thermore, the fractions adsorbed on IMAC-Ca2+(Fe3+) were separated and identified with reverse-phase (RP)-HPLC and MALDI-TOF MS/MS. The results showed that the sequence of peptides from FCa-2and FFe-3fractions was DEGEQPRPFPFP.