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Preparation of sheep bone collagen peptide–calcium chelate using enzymolysis-fermentation methodology and its structural characterization and stability analysis

机译:使用酶解 - 发酵方法的绵羊骨胶原蛋白肽 - 钙螯合物的制备及其结构特征及稳定性分析

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In this study, enzymatic hydrolysis and Lactobacillus fermentation were used in combination to prepare collagen peptide with high free calcium content, followed by the addition of anhydrous ethanol to obtain peptide–calcium chelate. The optimal conditions for the fermentation of enzymatic hydrolysate (glucose 3%, inoculum size 6%, 24.5 h, 37 °C and pH 6.5) were determined by response surface methodology (RSM), under which a free calcium content of 2212.58 mg/100 g was obtained. The calcium–chelating capacity was 42.57 ± 0.09%. The results of ultraviolet absorption spectrum, Fourier transform infrared (FT-IR) spectra, differential scanning calorimeter (DSC), X-ray diffraction and amino acid analysis indicated that calcium could be chelated through carboxyl oxygen and amino nitrogen atoms of collagen peptides, forming peptide–calcium chelate. The chelate is stable at 30–80 °C of temperatures and during in simulated gastrointestinal digestion, which could promote calcium absorption in human. The test intended to provide a basis for developing a novel calcium supplement and promoting utilization of sheep bone.
机译:在本研究中,使用酶水解和乳杆菌发酵组合以使胶原蛋白肽加入高钙含量,然后加入无水乙醇以获得肽 - 钙螯合物。通过响应表面方法(RSM)测定酶水解产物发酵(葡萄糖3%,接种物尺寸6%,24.5小时)的最佳条件(葡萄糖3%,接种物尺寸6%,37℃,37℃,37℃,37℃和pH6.5),其中游离钙含量为2212.58mg / 100获得了g。钙螯合能力为42.57±0.09%。紫外线吸收光谱,傅里叶变换红外(FT-IR)光谱,差示扫描量热仪(DSC),X射线衍射和氨基酸分析结果表明,钙可以通过羧基氧和胶原肽的氨基氮原子螯合,形成肽 - 钙螯合物。螯合物在30-80°C的温度和模拟胃肠消化期间稳定,可以促进人类的钙吸收。试验旨在为开发新型钙补充剂和促进羊骨的利用提供依据。

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