Yuejie Teng, Tingting Liu, Tianxiang Wang, Yuanyuan Dong, Da Ao, Guanghua Yang, Zhiqiang Cai
{"title":"新型菌株 Lichtheimia sp. UV-16 产生的外聚半乳糖脲酶及其水解特性","authors":"Yuejie Teng, Tingting Liu, Tianxiang Wang, Yuanyuan Dong, Da Ao, Guanghua Yang, Zhiqiang Cai","doi":"10.1021/acs.jafc.4c07818","DOIUrl":null,"url":null,"abstract":"A pectinase-producing strain, <i>Lichtheimia</i> sp. X-8, was isolated from the soil for the first time. Subsequently, <i>Lichtheimia</i> sp. UV-16, with a 1.23-fold increase in pectinase activity, was obtained via UV mutagenesis, and optimization of its liquid fermentation process boosted pectinase activity from 455.6 ± 12.7 to 3202.0 ± 82.1 U/mL. The crude enzyme was purified by salting out and anion exchange resin, with a purification ratio of 2.28-fold and a yield of 36.5%. The optimal reaction temperature for the pure enzyme was 60 °C with an optimal pH of 5.5. Thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC) confirmed that the enzyme was an exopolygalacturonase, achieving over 99% efficiency in pectin hydrolysis. Furthermore, incorporating pure enzymes into juice pulps can substantially enhance the juice yield, which makes this polygalacturonase a promising application in the beverage industry.","PeriodicalId":41,"journal":{"name":"Journal of Agricultural and Food Chemistry","volume":"84 1","pages":""},"PeriodicalIF":5.7000,"publicationDate":"2024-12-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Exopolygalacturonase Production from the Novel Strain Lichtheimia sp. UV-16 and Enzyme Hydrolysis Properties\",\"authors\":\"Yuejie Teng, Tingting Liu, Tianxiang Wang, Yuanyuan Dong, Da Ao, Guanghua Yang, Zhiqiang Cai\",\"doi\":\"10.1021/acs.jafc.4c07818\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"A pectinase-producing strain, <i>Lichtheimia</i> sp. X-8, was isolated from the soil for the first time. Subsequently, <i>Lichtheimia</i> sp. UV-16, with a 1.23-fold increase in pectinase activity, was obtained via UV mutagenesis, and optimization of its liquid fermentation process boosted pectinase activity from 455.6 ± 12.7 to 3202.0 ± 82.1 U/mL. The crude enzyme was purified by salting out and anion exchange resin, with a purification ratio of 2.28-fold and a yield of 36.5%. The optimal reaction temperature for the pure enzyme was 60 °C with an optimal pH of 5.5. Thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC) confirmed that the enzyme was an exopolygalacturonase, achieving over 99% efficiency in pectin hydrolysis. Furthermore, incorporating pure enzymes into juice pulps can substantially enhance the juice yield, which makes this polygalacturonase a promising application in the beverage industry.\",\"PeriodicalId\":41,\"journal\":{\"name\":\"Journal of Agricultural and Food Chemistry\",\"volume\":\"84 1\",\"pages\":\"\"},\"PeriodicalIF\":5.7000,\"publicationDate\":\"2024-12-17\",\"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://doi.org/10.1021/acs.jafc.4c07818\",\"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://doi.org/10.1021/acs.jafc.4c07818","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}
Exopolygalacturonase Production from the Novel Strain Lichtheimia sp. UV-16 and Enzyme Hydrolysis Properties
A pectinase-producing strain, Lichtheimia sp. X-8, was isolated from the soil for the first time. Subsequently, Lichtheimia sp. UV-16, with a 1.23-fold increase in pectinase activity, was obtained via UV mutagenesis, and optimization of its liquid fermentation process boosted pectinase activity from 455.6 ± 12.7 to 3202.0 ± 82.1 U/mL. The crude enzyme was purified by salting out and anion exchange resin, with a purification ratio of 2.28-fold and a yield of 36.5%. The optimal reaction temperature for the pure enzyme was 60 °C with an optimal pH of 5.5. Thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC) confirmed that the enzyme was an exopolygalacturonase, achieving over 99% efficiency in pectin hydrolysis. Furthermore, incorporating pure enzymes into juice pulps can substantially enhance the juice yield, which makes this polygalacturonase a promising application in the beverage industry.
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.