表面改性
辐照
化学
氧化磷酸化
激进的
劈理(地质)
半胱氨酸
肽
化学改性
二硫键
硫醇
紫外线照射
降级(电信)
翻译后修饰
光化学
酶
有机化学
生物化学
材料科学
复合材料
核物理学
物理化学
物理
电信
断裂(地质)
计算机科学
作者
Laura Fitzner,Toni Kühl,Mario Hasler,Diana Imhof,Karin Schwarz,Julia K. Keppler
出处
期刊:Food Chemistry
[Elsevier]
日期:2023-12-01
卷期号:428: 136698-136698
被引量:1
标识
DOI:10.1016/j.foodchem.2023.136698
摘要
Ultraviolet (UV) B irradiation induces protein modification, especially the conformational rearrangement of proteins, and is therefore promising as a non-thermal and non-chemical functionalization technique. Nevertheless, UVB irradiation introduces radicals and oxidizes side chains resulting in the loss of food quality. Thus, assessing the UVB irradiation-based functionalization of β-lactoglobulin (BLG) versus its oxidative degradation is of interest. UVB irradiation of up to 8 h was successfully applied to loosen the rigid folding of BLG and increase its flexibility. Thereby, the cysteine at position 121 and hydrophobic regions became surface-exposed as indicated by the increase in accessible thiol groups and increased surface hydrophobicity. Furthermore, we demonstrated the cleavage of the "outer" disulfide bond C66-C160 by LC-MS/MS after tryptic digestion of BLG. The 2-h-irradiated BLG showed adequate conformational rearrangement for protein functionalization while being minimally oxidized.
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