文献类型：期刊文献

英文题名：Oxidative polymerization of hydroxytyrosol catalyzed by laccase, tyrosinase or horseradish peroxidase: influencing factors and molecular simulations

作者：Xie, Pujun[1,2,3,4] Fan, Linlin[5] Huang, Lixin[2,3,4] Zhang, Caihong[2,3,4]

第一作者：谢普军;Xie, Pujun

通信作者：Huang, LX[1]|[a000570f79d3438a5c2bd]黄立新;

机构：[1]Chinese Acad Forestry, Inst New Technol Forestry, Beijing, Peoples R China;[2]Chinese Acad Forestry, Inst Chem Ind Forest Prod, 16 Suojin Wucun, Nanjing 210042, Jiangsu, Peoples R China;[3]Natl Engn Lab Biomass Chem Utilizat, Nanjing, Peoples R China;[4]Natl Forestry & Grassland Adm, Key & Open Lab Forest Chem Engn, Key Lab Biomass Energy & Mat, Nanjing, Peoples R China;[5]JAAS, Inst Agroprod Proc, Nanjing, Peoples R China

年份：2021

卷号：39

期号：15

起止页码：5486-5497

外文期刊名：JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS

收录：;Scopus(收录号：2-s2.0-85089258213);WOS:【SCI-EXPANDED(收录号:WOS:000557956200001)】；

基金：Funding support of this study was derived from Fundamental Research Funds of CAF (grant no. CAFYBB2020SY036), Natural Science Foundation of China (grant no. 31800614) and Jiangsu Provincial Natural Science Foundation of China (grant no. BK20181124).

语种：英文

外文关键词：Laccase; enzymatic polymerization; hydroxytyrosol oligomers; process parameters; molecular dockings and dynamics

摘要：Hydroxytyrosol oligomer from bioenzymatic catalysis indicates a pleiotropic wellness improving (e.g. antioxidation, anti-inflammatory and anti-carcinogenesis) than its monomer. However, the processing parameters and the insightful mechanism of hydroxytyrosol polymerization are still lacking. To explore in detail the process of hydroxytyrosol polymerization, the effects of different reaction factors (solvent type, pH value of reaction solution, reaction temperature and time) on the polymerization yield were investigated, and molecular docking was executed to reveal the relevant structural variations of these enzymes. The results showed hydroxytyrosol polymerization implemented by laccase performed the best at 50 degrees C for 20 min in the aqueous buffer solution of pH 5.0. The docking results demonstrated PRO4, TYR7, ASP8, PRO12, LEU121 and VAL14 in site 9 of laccase interacted with hydroxytyrosol in hydrogen bonding, pi-sigma, pi-alkyl and van der Waals' force. Moreover, the molecular dynamic results implied their interaction-energy variation reaching balance within 175ps, which confirmed the enzymes' structural changes. Meanwhile, structural analysis in torsion and bond lengths showed that the C-O of phenolic bonds from hydroxytyrosol evidently rotated and its length of the relevant O-H became longer when binding to laccase compared with free hydroxytyrosol. All the findings are helpful to strengthen the understanding for the enzymatic polymerization of catechol-based structures and the resultingo-dihydroxy-grafting oligomers could be potentially used in the field of functional foods, cosmetics and pharmaceuticals, even or an innovative bioenzyme design such as biosensor for measuring phenols in industrial effluent or preparing the singular oligomer oriented is worth being explored in future. Communicated by Ramaswamy H. Sarma