College of Agricultural and Bioresources, University of Saskatchewan Saskatoon, SK S7N 5AB, Canada.
J Dairy Sci. 2011 Dec;94(12):6092-102. doi: 10.3168/jds.2011-4619.
Heat processing has been used to improve protein utilization and availability of animal nutrition. However, to date, few studies exist on heat-induced protein molecular structure changes on a molecular basis. The aims of this study were to use molecular spectroscopy as a novel approach to determine heat-induced protein molecular structure changes affected by moist and dry heating and quantify protein molecular structures and nutritive value in the rumen and intestine in dairy cattle. In this study, soybean was used as a model for feed protein and was autoclaved at 120°C for 1h (moist heating) and dry heated at 120°C for 1h. The parameters assessed in this study included protein structure α-helix and β-sheet and their ratio, protein subfractions associated with protein degradation behaviors, intestinal protein availability, and energy values. The results show that heat treatments changed the protein molecular structure. Both dry and moist heating increased the amide I-to-amide II ratio. However, for the protein α-helix-to-β-sheet ratio, moist heating decreased but dry heating increased the ratio. Compared with dry heating, moist heating dramatically changed the chemical and nutrient profiles of soybean seed. It greatly decreased soluble crude protein, nonprotein nitrogen, and increased neutral detergent insoluble protein. Both dry and moist heating treatments did not alter digestible nutrients and energy values. Heating tended to decrease the nonprotein nitrogen fraction (soluble and rapidly degradable protein fraction) and true protein 1 fraction (fast-degradable protein fraction). Conversely, the true protein 3 fraction (slowly degradable fraction) significantly increased. The in situ rumen study showed that moist heating decreased protein rumen degradability and increased intestinal digestibility of rumen-undegradable protein. Compared with the raw soybeans, dry heating did not affect rumen degradability and intestinal digestibility. In conclusion, compared with dry heating, moist heating dramatically affected the nutrient profile, protein subfractions, rumen degradability, intestinal digestibility, and protein molecular structure (amide I-to-II ratio; α-helix-to-β-sheet ratio). The sensitivity of soybean seed to moist heating was much higher than that to dry heating in terms of the structure and nutrient profile changes.
热处理已被用于改善动物营养中的蛋白质利用率和可用性。然而,迄今为止,关于热诱导蛋白质分子结构变化的基础研究很少。本研究旨在使用分子光谱学作为一种新方法,确定湿热和干热对蛋白质分子结构的影响,并量化奶牛瘤胃和肠道中蛋白质的分子结构和营养价值。在本研究中,大豆被用作饲料蛋白的模型,并在 120°C 下湿热 1 小时(湿热)和干热 1 小时。本研究评估的参数包括蛋白质结构α-螺旋和β-折叠及其比例、与蛋白质降解行为相关的蛋白质亚基、肠道蛋白质可利用性和能量值。结果表明,热处理改变了蛋白质分子结构。湿热和干热都增加了酰胺 I 与酰胺 II 的比值。然而,对于蛋白质α-螺旋与β-折叠的比例,湿热降低,干热增加。与干热相比,湿热极大地改变了大豆种子的化学和营养特性。它大大降低了可溶性粗蛋白、非蛋白氮,增加了中性洗涤剂不溶蛋白。湿热和干热处理都没有改变可消化养分和能量值。加热倾向于降低非蛋白氮部分(可溶性和快速降解蛋白部分)和真蛋白 1 部分(快速降解蛋白部分)。相反,真蛋白 3 部分(缓慢降解部分)显著增加。瘤胃原位研究表明,湿热降低了蛋白质瘤胃降解率,增加了肠道对瘤胃未降解蛋白的消化率。与生大豆相比,干热处理对瘤胃降解率和肠道消化率没有影响。总之,与干热相比,湿热对营养成分、蛋白质亚基、瘤胃降解率、肠道消化率和蛋白质分子结构(酰胺 I 与酰胺 II 的比值;α-螺旋与β-折叠的比值)有显著影响。就结构和营养成分变化而言,大豆种子对湿热的敏感性远高于干热。