期刊
FOOD CHEMISTRY
卷 315, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2020.126228
关键词
Monascin; Bovine serum albumin; Interaction; Antioxidant activity
资金
- National Natural Science Foundation of China [21506152]
- Natural Science Foundation of Tianjin [19JCYBJC21000]
- Foundation of Tianjin Engineering Research Center of Safety Control Technology in Food Processing, China [GCZX201803]
- project program of Key Laboratory of Food Nutrition and Safety, Ministry of Education, China [2018003]
- Key Project of Tianjin Education Commission Scientific Research Plan [2017KJ004]
- Project from Tianjin University of Science Technology [2016LG02]
Monascin (MS) is a yellow lipid-soluble azaphilonoid pigment identified from Monascus-fermented products with promising biological activities. This work studied interactions between MS and bovine serum albumin (BSA) as well as their influences on the antioxidant activity of MS. Experimental results demonstrated that the fluorescence emission of BSA was quenched by MS via static quenching mechanism and the formed BSA-MS complex was mainly maintained by hydrophobic and hydrogen bond interactions. Meanwhile, the probable binding pocket of MS located near site I of BSA and the corresponding conformational and structural alterations of BSA were determined. Furthermore, the molecular modeling approach was performed to understand the visual representation of binding mode between BSA and MS. It was noticeable that the BSA-MS complex exhibited reduced DPPH radical-scavenging ability, which might be attributed to the restraining effect of BSA on the relevant reaction pathways involved in antioxidation by MS.
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