摘要
为探究丙酮和正己烷对橡胶籽β-葡萄糖苷酶活性及热稳定性的影响,测定了橡胶籽β-葡萄糖苷酶在不同体积分数的丙酮和正己烷溶液中酶活及热稳定性的变化情况。低体积分数(φ<10%)丙酮可提升β-葡萄糖苷酶酶活,体积分数大于10%后,随着体积分数提升残余酶活降低。任意体积正己烷都会抑制酶活。酶在丙酮-水溶液中热稳定性下降;当水-正己烷溶液中正己烷体积分数较低时(φ<10%),随着加热时间增加,酶热稳定性增强。通过AutoDock Tools研究了橡胶籽β-葡萄糖苷酶与丙酮分子和正己烷分子之间的对接情况,结果发现丙酮能与酶蛋白的活性位点深处的氨基酸残基相互作用,而正己烷主要与酶蛋白的催化口袋附近的氨基酸残基相互作用。该研究结果可为含有有机溶剂的催化体系中β-葡萄糖苷酶的应用提供一定的理论依据。
In order to study the effect of acetone and n-hexane on enzyme activity and thermal stability of β-glucosidase from Rubber Seeds,the changes of β-glucosidase in different volume fractions of acetone and n-hexane were measured experimentally.Acetone with lower volume fraction (φ<10%) could activate β-glucosidase activity,when the volume fraction was greater than 10%,the residual enzyme activity decreased with the increased of the volume fraction.n-Hexane inhibited β-glucosidase activity.The thermal stability of enzyme in acetone-water solution decreased.When the volume fraction of n-hexane in water-n-hexane solution is lower (φ<10%),the thermal stability of β-glucosidase can be enhanced with the increase of heating time.The docking of β-glucosidase with acetone molecules and n-hexane molecules was studied by AutoDock Tools,the docking results show that acetone can interact with amino acid residues deep in the active site of the enzyme protein,while n-hexane mainly interacted with amino acid residues near the catalytic pocket of the enzyme protein.The research results can provide some theoretical basis for the application of β-glucosidase in catalytic system containing organic solvent.
作者
徐佳茜
邓皓嘉
刘石生
XU Jiaqian;DENG Haojia;LIU Shisheng(Engineering Research Center of Utilization of Tropical Polysaccharide Resources,Ministry of Education,Haikou 570228,China;College of Food Science and Engineering,Hainan University,Haikou 570228,China)
出处
《食品科技》
CAS
北大核心
2020年第4期219-225,共7页
Food Science and Technology
基金
国家自然科学基金项目(31460407)。
