文献类型： 外文期刊
作者： Lu, Jing 1 ; Liu, Shuangneng 1 ; Wei, Miaohong 2 ; Zhang, Wenyuan 2 ; Zhu, Tong 1 ; Xing, Lina 1 ; Liu, Jinqi 1 ; Zheng, Xiaowei 3 ; Pang, Xiaoyang 2 ; Zhang, Shuwen 2 ; Lv, Jiaping 2 ;
作者机构： 1.Beijing Technol & Business Univ, Beijing Adv Innovat Ctr Food Nutr & Human Hlth, Beijing Engn & Technol Res Ctr Food Addit, Sch Food & Hlth, Beijing 100048, Peoples R China
2.Chinese Acad Agr Sci, Inst Food Sci & Technol, Beijing 100193, Peoples R China
3.COFCO Corp, Nutr & Hlth Res Inst, Beijing 102209, Peoples R China
关键词： Lactotransferrin; Heating; Lactosylation; In-vitro digestion
期刊名称：FOOD CHEMISTRY （ 影响因子：9.8； 五年影响因子：9.7 ）
ISSN： 0308-8146
年卷期： 2025 年 465 卷
页码：
收录情况： SCI
摘要： Lactosylation of lysines occurs during the heating of dairy products, yet how lactosylation impact the lysine release during digestion remains largely unknown. This study examines the effect of lactosylation on the digestibility of lactotransferrin using chemical analysis, proteomics, and peptidomics. Under the applied heating conditions, lactotransferrin primarily undergoes early-stage Maillard reactions, producing lactulose-lysine. Furosine content increases with heating time and temperature, with time being more influential. And 23 out of 54 lysines in lactotransferrin were lactosylated. Following in-vitro infant digestion, free lysine levels in samples heated at 130 degrees C for 30s decreased by 25 % compared to unheated ones, likely due to lactosylation hindering protease cleavage. Intriguingly, lactosylated lysine was absent in peptides ranging from 5 to 17 amino acids but remained in larger peptides. The formation of large lactosylated peptides from heating impeded free lysine release. Further investigation is needed to determine if the human body can utilize these lactosylated peptides.
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