新型啤酒稳定剂对啤酒蛋白质吸附特性的研究
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  • 英文篇名:Research on the Adsorption Character of New Beer Stabilizer to Beer Protein
  • 作者:唐栋健 ; 郑飞云 ; 马军涛 ; 成贵 ; 朱林 ; 李永仙 ; 李崎
  • 英文作者:TANG Dongjian;ZHENG Feiyun;MA Juntao;CHEN Gui;ZHU Linjiang;LI Yongxian;LI Qi;The Key Laboratory of Industrial Biotechnology of Ministry of Education,Jiangnan University;Hongzhi New Material Technology(Liyang) Co.,Ltd;
  • 关键词:BFSA ; 啤酒蛋白质 ; 吸附 ; 动力学 ; 热力学
  • 英文关键词:BFSA;;beer protein;;adsorption;;kinetics;;thermodynamics
  • 中文刊名:WXQG
  • 英文刊名:Journal of Food Science and Biotechnology
  • 机构:江南大学教育部工业生物技术重点实验室;溧阳市鸿智新材料科技有限公司;
  • 出版日期:2019-01-15
  • 出版单位:食品与生物技术学报
  • 年:2019
  • 期:v.38;No.226
  • 基金:国家863计划(2013AA102106-03);; 国家自然科学基金项目(31271919,31571942,31301539,31601558,31601445);; 江苏高校优势学科建设工程资助项目(PAPD);; 江苏省自然科学基金项目(BK20150159);; 江苏基础研究资助项目(JUSRP51306A,JUSRP51402A&JUDCF13008)
  • 语种:中文;
  • 页:WXQG201901015
  • 页数:6
  • CN:01
  • ISSN:32-1751/TS
  • 分类号:74-79
摘要
研究了新型啤酒稳定剂BFSA对啤酒蛋白质的吸附特性,初步探讨了BSFA吸附蛋白的作用机理。FT-IR图谱分析可知,BFSA表面含有Si-O-Si键,且含有O-H键。研究了时间、温度、蛋白质浓度对BFSA吸附的影响,发现吸附平衡时间在1 h左右,BFSA吸附啤酒蛋白质量随温度的降低而升高,随着初始蛋白质浓度的升高而升高。研究了BFSA吸附啤酒蛋白质的吸附等温线、动力学和热力学模型,发现BFSA对啤酒蛋白质的吸附等温线更符合Freundlich方程;对啤酒蛋白质的吸附过程更符合准二级动力学方程;由热力学参数ΔG>0说明啤酒蛋白质在BFSA表面的吸附为非自发的,ΔH<0说明吸附过程是放热的,ΔS<0说明吸附是熵减过程;活化能(E)为26.28 kJ/mol表明BFSA吸附啤酒蛋白质是物理吸附;吸附过程放热为6.62 kJ/mol表明该吸附过程的主要作用力可能是范德华力、氢键和疏水作用。
        Research on the adsorption character of BFSA to beer protein and adsorption mechanism of BFSA. FT-IR spectrum analysis showed that the surface contained not only Si-O-Si bond,but also O-H bond. Research on the influence of adsorption time,temperature and protein concentration on BFSA,the result showed that adsorption equilibrium time was 1 h and the adsorption amount of BFSA decreased with temperature increased and increased with protein concentration increased. The adsorption isotherm,kinetics and thermodynamics of protein on BFSA surface were studied by batch equilibrium experiments;The result showed the adsorption of BFSA was fitted to Freundlich isotherm equation;The adsorption process followed the pseudo-second-order kinetic model;The thermodynamic parameters were obtained as ΔG>0 indicated that the adsorption was a non-spontaneous process,ΔH<0 indicated that the adsorption was exothermic,ΔS<0 indicated that the adsorption was an entropy-decreasing process;The values of E was 26.28 KJ/mol indicated that the adsorption process was physical adsorption;The heat release of adsorption was 6.62 KJ/mol implied that Van der Waals forces hydrogen bond and hydrophobic bond were responsible for the binding of protein with BFSA.
引文
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