Purification and characterization of caclium-binding soybean protein hydrolysates by Ca²⁺/Fe³⁺ immobilized metal affinity chromatography (IMAC)

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• 作者：Ying Lv ; Xiaolan Bao ; He Liu ; Jianhua Ren ; Shuntang Guo
• 关键词：Purification ; Characterization ; Soybean protein hydrolysates ; Calcium binding ; Amino acid composition ; IMAC
• 刊名：Food Chemistry
• 出版年：2013
• 出版时间：1 December, 2013
• 年：2013
• 卷：141
• 期：3
• 页码：1645-1650
• 全文大小：606 K

文摘

Soybean protein hydrolysates (SPHs) can bind calcium in order to form soluble peptide-calcium complexes. 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 chromatography (IMAC), and examined the effects of SPHs with different amino acid composition on calcium binding capacity. Three fractions (F_Fe-1, F_Fe-2 and F_Fe-3) isolated with IMAC-Fe³⁺ were shown possessing increased Glu, Gln, Lys and Pro content from F_Fe-1 to F_Fe-3, and improved amount of bound calcium. Furthermore, 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 F_Ca-2 and F_Fe-3 fractions was DEGEQPRPFPFP.