Food and Fermentation Industries >

2020 , Vol. 46 >Issue 11: 61 - 68

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.022733

Study on the mechanism of interactions between bovine serum albuminwith o-dihydroxybenzene and m-trihydroxybenzene

  • CHU Qianqian ,
  • AI Jian ,
  • FANG Jiaqi ,
  • HAN Qiuyu ,
  • BAO Bin ,
  • SUN Yongjun
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  • 1(College of Food Science and Technology,Shanghai Ocean University,Shanghai 201306,China)
    2(National Experimental Teaching Demonstration Center for Food Science and Engineering (Shanghai Ocean University),Shanghai 201306,China)
    3(Good Master Group Co., Ltd., Rongcheng 264305, China)

Received date: 2019-11-06

  Online published: 2020-06-24

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Abstract

This study aimed to investigate the interaction mechanism between phenolic compounds and proteins. The o-dihydroxybenzene (OP) and m-trihydroxybenzene (MP) were oxidized under alkaline conditions in the presence of oxygen to obtain oxidized o-dihydroxybenzene (OOP) and oxidized m-trihydroxybenzene (OMP), which were respectively reacted with oxidized and unoxidized OP, MP and BSA at room temperature. The changes of free amino, sulfhydryl, non-covalent interaction and surface hydrophobicity between BSA and OP, MP, OOP and OMP were analyzed. Changes were characterized by Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD) and differential scanning calorimeter (DSC). The results showed that the content of free amino and sulfhydryl groups did not change significantly between BSA and OP and MP, but OOP and OMP could significantly reduce the content of free amino and sulfhydryl groups in BSA.AndthereductionofOOP-BSA was greater than that of OMP-BSA. Moreover, MP can form hydrogen bonds with BSA, but the ionic bond did not change significantly and the increase of MP-BSA hydrogen bond was greater than that of OP-BSA. After the reaction between OP and BSA, the hydrophobic interaction increased significantly. While MP caused the hydrophobic interaction to decrease significantly. Furthermore, OP, MP, OOP, OMP could significantly reduce the hydrophobicity of BSA surface and the reduction of OP-BSA, OOP-BSA was greater than MP-BSA, OMP-BSA. FTIR and CD results showed that OP, MP, OOP, OMP could change the secondary structure of BSA which was characterized by the decreased α-helix content and increased β-sheet, β-turn and random coil. The effects of OP and OOP were greater than those of MP and OMP. DSC results showed that the introduction of OP, MP, OOP and OMP increased the thermal denaturation temperature of BSA. These results indicated that catechol and phloroglucinol undergo oxidative interaction with BSA and unoxidized catechol and phloroglucinol could interact non-covalently with bovine serum albumin. These interactions may alter the functional properties of the protein, thereby affecting the application of the protein in food.

Key words： o-dihydroxybenzene; m-trihydroxybenzene; protein; covalent interaction; non-covalent interaction

Cite this article

CHU Qianqian , AI Jian , FANG Jiaqi , HAN Qiuyu , BAO Bin , SUN Yongjun . Study on the mechanism of interactions between bovine serum albuminwith o-dihydroxybenzene and m-trihydroxybenzene[J]. Food and Fermentation Industries, 2020 , 46(11) : 61 -68 . DOI: 10.13995/j.cnki.11-1802/ts.022733

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