Micaela Baglioni, Alexander Fries, Javier D. Breccia, Laura S. Mazzaferro
{"title":"引导商业糖苷酶制剂对生产芦丁糖的选择性","authors":"Micaela Baglioni, Alexander Fries, Javier D. Breccia, Laura S. Mazzaferro","doi":"10.1016/j.procbio.2024.06.022","DOIUrl":null,"url":null,"abstract":"<div><p>Aromase™ H2 is an enzymatic cocktail marketed to intensify the aroma, promote clarity and overall flavor of tea by releasing aromatic compounds and antioxidants that are naturally glycosylated. The hydrolysis of a wide range of glycoconjugates is the key to its action, which can arise from the substrate promiscuity of the main diglycosidase or other enzymes that are in the mixture. The characterization focusing on the activity toward flavonoids at different pH values allowed to increase the cocktail ratio of diglycosidase to α-rhamnosidase activity. In that way, the free disaccharide rutinose was selectively obtained in a laboratory scale reactor with 90 % conversion after 3.5 h reaction at pH 8. Purification was carried out by liquid-liquid extraction, recovering the aglycone hesperetin. Subsequent extraction with activated carbon allowed a recovery of 84 % of the rutinose. This work demonstrates the practical application of a commercial cocktail for the selective hydrolysis of rutinosylated compounds.</p></div>","PeriodicalId":20811,"journal":{"name":"Process Biochemistry","volume":null,"pages":null},"PeriodicalIF":3.7000,"publicationDate":"2024-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Guiding the selectivity of commercial glycosidase preparation towards the production of rutinose\",\"authors\":\"Micaela Baglioni, Alexander Fries, Javier D. Breccia, Laura S. Mazzaferro\",\"doi\":\"10.1016/j.procbio.2024.06.022\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Aromase™ H2 is an enzymatic cocktail marketed to intensify the aroma, promote clarity and overall flavor of tea by releasing aromatic compounds and antioxidants that are naturally glycosylated. The hydrolysis of a wide range of glycoconjugates is the key to its action, which can arise from the substrate promiscuity of the main diglycosidase or other enzymes that are in the mixture. The characterization focusing on the activity toward flavonoids at different pH values allowed to increase the cocktail ratio of diglycosidase to α-rhamnosidase activity. In that way, the free disaccharide rutinose was selectively obtained in a laboratory scale reactor with 90 % conversion after 3.5 h reaction at pH 8. Purification was carried out by liquid-liquid extraction, recovering the aglycone hesperetin. Subsequent extraction with activated carbon allowed a recovery of 84 % of the rutinose. This work demonstrates the practical application of a commercial cocktail for the selective hydrolysis of rutinosylated compounds.</p></div>\",\"PeriodicalId\":20811,\"journal\":{\"name\":\"Process Biochemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":3.7000,\"publicationDate\":\"2024-06-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Process Biochemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1359511324002083\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Process Biochemistry","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1359511324002083","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Guiding the selectivity of commercial glycosidase preparation towards the production of rutinose
Aromase™ H2 is an enzymatic cocktail marketed to intensify the aroma, promote clarity and overall flavor of tea by releasing aromatic compounds and antioxidants that are naturally glycosylated. The hydrolysis of a wide range of glycoconjugates is the key to its action, which can arise from the substrate promiscuity of the main diglycosidase or other enzymes that are in the mixture. The characterization focusing on the activity toward flavonoids at different pH values allowed to increase the cocktail ratio of diglycosidase to α-rhamnosidase activity. In that way, the free disaccharide rutinose was selectively obtained in a laboratory scale reactor with 90 % conversion after 3.5 h reaction at pH 8. Purification was carried out by liquid-liquid extraction, recovering the aglycone hesperetin. Subsequent extraction with activated carbon allowed a recovery of 84 % of the rutinose. This work demonstrates the practical application of a commercial cocktail for the selective hydrolysis of rutinosylated compounds.
期刊介绍:
Process Biochemistry is an application-orientated research journal devoted to reporting advances with originality and novelty, in the science and technology of the processes involving bioactive molecules and living organisms. These processes concern the production of useful metabolites or materials, or the removal of toxic compounds using tools and methods of current biology and engineering. Its main areas of interest include novel bioprocesses and enabling technologies (such as nanobiotechnology, tissue engineering, directed evolution, metabolic engineering, systems biology, and synthetic biology) applicable in food (nutraceutical), healthcare (medical, pharmaceutical, cosmetic), energy (biofuels), environmental, and biorefinery industries and their underlying biological and engineering principles.