School of Food and Nutritional Sciences, University College Cork, Cork, Ireland.
Nestlé Research, Nestlé Institute of Health Sciences, Vers-chez-les-Blanc, CH-1000 Lausanne 26, Switzerland.
Food Chem. 2021 Nov 15;362:130142. doi: 10.1016/j.foodchem.2021.130142. Epub 2021 May 18.
Lactoferrin (LF) is a multifunctional glycoprotein which, when thermally processed, undergoes significant physicochemical changes. The link between such changes and the bioactivity of LF is not well characterised and requires much research. In this work, bovine LF solutions (1%, w/v, protein, pH 7) were thermally processed using high temperature short time conditions (72, 80, 85 or 95 °C with 15 s holding times). Following this, it was shown that LF and heat induced LF aggregates were largely resistant to simulated infant gastric, but not intestinal, digestion. Also, the efficacy of LF bactericidal activity, and inhibition of lipopolysaccharide-induced NF-κB activation were negatively impacted by thermal processing. This study confirmed that the efficacy of LF bio-functionalities was affected by the extent of heat-induced changes in protein structure whereby processing conditions of least severity (i.e. pasteurisation) had the least impact on bioactivity.
乳铁蛋白（LF）是一种多功能糖蛋白，经热处理后会发生显著的物理化学变化。这种变化与 LF 生物活性之间的联系还没有很好地表征，需要进行大量的研究。在这项工作中，使用高温短时间处理条件（72、80、85 或 95°C 并保持 15s）对 1%（w/v，蛋白质，pH7）的牛乳铁蛋白溶液进行热处理。结果表明，LF 和热诱导的 LF 聚集体在很大程度上能抵抗模拟婴儿胃消化，但不能抵抗肠道消化。此外，LF 的杀菌活性和抑制脂多糖诱导的 NF-κB 激活的功效受到热处理的负面影响。这项研究证实，LF 生物功能的功效受到热诱导的蛋白质结构变化程度的影响，其中最温和的处理条件（即巴氏杀菌）对生物活性的影响最小。
