Mingtao Zhao, Baohui Zhang, Xiaofeng Wu and Yi Xiao*,
{"title":"在大肠杆菌中从 L-酪氨酸高效合成单木质素的全细胞生物转化系统。","authors":"Mingtao Zhao, Baohui Zhang, Xiaofeng Wu and Yi Xiao*, ","doi":"10.1021/acs.jafc.4c02611","DOIUrl":null,"url":null,"abstract":"<p >Monolignols and their derivatives exhibit various pharmaceutical and physiological characteristics, such as antioxidant and anti-inflammatory properties. However, they remain difficult to synthesize. In this study, we engineered several whole-cell bioconversion systems with carboxylate reductase (CAR)-mediated pathways for efficient synthesis of <i>p</i>-coumaryl, caffeyl, and coniferyl alcohols from <span>l</span>-tyrosine in <i>Escherichia coli</i> BL21 (DE3). By overexpressing the <span>l</span>-tyrosine ammonia lyase from <i>Flavobacterium johnsoniae</i> (FjTAL), carboxylate reductase from <i>Segniliparus rugosus</i> (SruCAR), alcohol dehydrogenase YqhD and hydroxylase HpaBC from <i>E. coli</i>, and caffeate 3-O-methyltransferase (COMT) from <i>Arabidopsis thaliana</i>, three enzyme cascades FjTAL–SruCAR–YqhD, FjTAL–SruCAR–YqhD–HpaBC, and FjTAL–SruCAR–YqhD–HpaBC–COMT were constructed to produce 1028.5 mg/L <i>p</i>-coumaryl alcohol, 1015.3 mg/L caffeyl alcohol, and 411.4 mg/L coniferyl alcohol from 1500, 1500, and 1000 mg/L <span>l</span>-tyrosine, with productivities of 257.1, 203.1, and 82.3 mg/L/h, respectively. This work provides an efficient strategy for the biosynthesis of <i>p</i>-coumaryl, caffeyl, and coniferyl alcohols from <span>l</span>-tyrosine.</p>","PeriodicalId":41,"journal":{"name":"Journal of Agricultural and Food Chemistry","volume":null,"pages":null},"PeriodicalIF":5.7000,"publicationDate":"2024-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Whole-Cell Bioconversion Systems for Efficient Synthesis of Monolignols from L-Tyrosine in Escherichia coli\",\"authors\":\"Mingtao Zhao, Baohui Zhang, Xiaofeng Wu and Yi Xiao*, \",\"doi\":\"10.1021/acs.jafc.4c02611\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p >Monolignols and their derivatives exhibit various pharmaceutical and physiological characteristics, such as antioxidant and anti-inflammatory properties. However, they remain difficult to synthesize. In this study, we engineered several whole-cell bioconversion systems with carboxylate reductase (CAR)-mediated pathways for efficient synthesis of <i>p</i>-coumaryl, caffeyl, and coniferyl alcohols from <span>l</span>-tyrosine in <i>Escherichia coli</i> BL21 (DE3). By overexpressing the <span>l</span>-tyrosine ammonia lyase from <i>Flavobacterium johnsoniae</i> (FjTAL), carboxylate reductase from <i>Segniliparus rugosus</i> (SruCAR), alcohol dehydrogenase YqhD and hydroxylase HpaBC from <i>E. coli</i>, and caffeate 3-O-methyltransferase (COMT) from <i>Arabidopsis thaliana</i>, three enzyme cascades FjTAL–SruCAR–YqhD, FjTAL–SruCAR–YqhD–HpaBC, and FjTAL–SruCAR–YqhD–HpaBC–COMT were constructed to produce 1028.5 mg/L <i>p</i>-coumaryl alcohol, 1015.3 mg/L caffeyl alcohol, and 411.4 mg/L coniferyl alcohol from 1500, 1500, and 1000 mg/L <span>l</span>-tyrosine, with productivities of 257.1, 203.1, and 82.3 mg/L/h, respectively. This work provides an efficient strategy for the biosynthesis of <i>p</i>-coumaryl, caffeyl, and coniferyl alcohols from <span>l</span>-tyrosine.</p>\",\"PeriodicalId\":41,\"journal\":{\"name\":\"Journal of Agricultural and Food Chemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":5.7000,\"publicationDate\":\"2024-06-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Agricultural and Food Chemistry\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://pubs.acs.org/doi/10.1021/acs.jafc.4c02611\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"AGRICULTURE, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Agricultural and Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://pubs.acs.org/doi/10.1021/acs.jafc.4c02611","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}
Whole-Cell Bioconversion Systems for Efficient Synthesis of Monolignols from L-Tyrosine in Escherichia coli
Monolignols and their derivatives exhibit various pharmaceutical and physiological characteristics, such as antioxidant and anti-inflammatory properties. However, they remain difficult to synthesize. In this study, we engineered several whole-cell bioconversion systems with carboxylate reductase (CAR)-mediated pathways for efficient synthesis of p-coumaryl, caffeyl, and coniferyl alcohols from l-tyrosine in Escherichia coli BL21 (DE3). By overexpressing the l-tyrosine ammonia lyase from Flavobacterium johnsoniae (FjTAL), carboxylate reductase from Segniliparus rugosus (SruCAR), alcohol dehydrogenase YqhD and hydroxylase HpaBC from E. coli, and caffeate 3-O-methyltransferase (COMT) from Arabidopsis thaliana, three enzyme cascades FjTAL–SruCAR–YqhD, FjTAL–SruCAR–YqhD–HpaBC, and FjTAL–SruCAR–YqhD–HpaBC–COMT were constructed to produce 1028.5 mg/L p-coumaryl alcohol, 1015.3 mg/L caffeyl alcohol, and 411.4 mg/L coniferyl alcohol from 1500, 1500, and 1000 mg/L l-tyrosine, with productivities of 257.1, 203.1, and 82.3 mg/L/h, respectively. This work provides an efficient strategy for the biosynthesis of p-coumaryl, caffeyl, and coniferyl alcohols from l-tyrosine.
期刊介绍:
The Journal of Agricultural and Food Chemistry publishes high-quality, cutting edge original research representing complete studies and research advances dealing with the chemistry and biochemistry of agriculture and food. The Journal also encourages papers with chemistry and/or biochemistry as a major component combined with biological/sensory/nutritional/toxicological evaluation related to agriculture and/or food.