大豆蛋白
豌豆蛋白
化学
食品科学
细菌
消化(炼金术)
乳酸
水解
蛋白质亚单位
发酵
凝胶电泳
色谱法
生物化学
生物
遗传学
基因
作者
Yaqiong Wang,Wenjing Sun,Yi Zhang,Wei Li,Qiuqin Zhang,Xin Rui
标识
DOI:10.1016/j.foodhyd.2022.108309
摘要
Food matrix plays an important role in regulating macronutrient digestibility. In this study, lactic acid bacteria (LAB)-fermented soy protein isolates (FSPIs) were prepared at a series of concentration (0.2%–5.0%, w/v). FSPIs with varied structures were obtained and tested in an in vitro dynamic gastrointestinal model. Then, a comparative digestomics research was conducted. Results demonstrated that the lowest gelation concentration of soy protein during LAB fermentation was 1.9% (w/v). The FSPIs showed structures ranging from a loosely stacked layer (non-gel, NG) to a denser gel network with varied hardness (weak gel, WG; medium gel, MG; and firm gel, FG) when the protein concentration was adjusted. The protein profile of gastrointestinal digestates demonstrated higher soluble protein and peptide in FSPI gels compared with FSPI-NG. FSPI gel digestates were predominantly promoted in glycinin G1 and the β-conglycinin α subunit. The change was dynamic between FSPI gels with varied structures. Weaker gels (FSPI-WG and FSPI-MG) facilitated the hydrolysis of glycinin G1/G4 and β-conglycinin α/β subunits at early and medium digestions (0–30 min). In comparison, the firmer gel (FSPI-FG) showed a postponed but more extensive promotion of the degradation of glycinin G1/G2 and β-conglycinin α subunits at the late digestion (180 min). The spatial structures of glycinin G1 and β-conglycinin α subunits demonstrated variations in seven and eight regions, respectively. Glycinin's region 6 (Y374–R388) and β-conglycinin's region 7 (L491–T519), which are located at the interior of the 3D structure, were the key regions contributing to the discrepancies.
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