{"title":"分离、鉴定和优化利用香蕉皮废料生产酪氨酸酶的工业应用。","authors":"Raheela Jabeen, Ume Habiba, Tahmina Mustafa, Tayyeba Rehman","doi":"10.1080/14786419.2024.2426209","DOIUrl":null,"url":null,"abstract":"<p><p>The study aimed to isolate, purify and optimise tyrosinase from banana peel waste for industrial use. Tyrosinase was extracted from banana peel using phosphate buffer. Purification initiated with centrifugation followed by ammonium sulphate precipitation. Further purification and characterisation was done through gel filtration. Bradford assay was used to determine the protein concentration. Enzyme activity of each sample was measured using tyrosinase activity assay. The pH and temperature optimisation of tyrosinase were also obtained. Results indicated that fractions obtained through ammonium sulphate precipitation at 70% saturation showed more activity than that of crude extract and 35% saturated fractions. Gel filtration column results showed that fraction number 17 &18 have maximum activity. Tyrosinase showed maximum activity at pH 7.0; 37 °C. Comparison between industrially purified and lab-isolated enzyme showed that both have similar optimum pH and temperature. It can be concluded that banana peel can be a source for synthesis of tyrosinase.</p>","PeriodicalId":18990,"journal":{"name":"Natural Product Research","volume":" ","pages":"1-5"},"PeriodicalIF":1.9000,"publicationDate":"2024-11-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Isolation, identification and optimization for tyrosinase production by banana peel waste for industrial application.\",\"authors\":\"Raheela Jabeen, Ume Habiba, Tahmina Mustafa, Tayyeba Rehman\",\"doi\":\"10.1080/14786419.2024.2426209\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The study aimed to isolate, purify and optimise tyrosinase from banana peel waste for industrial use. Tyrosinase was extracted from banana peel using phosphate buffer. Purification initiated with centrifugation followed by ammonium sulphate precipitation. Further purification and characterisation was done through gel filtration. Bradford assay was used to determine the protein concentration. Enzyme activity of each sample was measured using tyrosinase activity assay. The pH and temperature optimisation of tyrosinase were also obtained. Results indicated that fractions obtained through ammonium sulphate precipitation at 70% saturation showed more activity than that of crude extract and 35% saturated fractions. Gel filtration column results showed that fraction number 17 &18 have maximum activity. Tyrosinase showed maximum activity at pH 7.0; 37 °C. Comparison between industrially purified and lab-isolated enzyme showed that both have similar optimum pH and temperature. It can be concluded that banana peel can be a source for synthesis of tyrosinase.</p>\",\"PeriodicalId\":18990,\"journal\":{\"name\":\"Natural Product Research\",\"volume\":\" \",\"pages\":\"1-5\"},\"PeriodicalIF\":1.9000,\"publicationDate\":\"2024-11-08\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Natural Product Research\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.1080/14786419.2024.2426209\",\"RegionNum\":3,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Natural Product Research","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1080/14786419.2024.2426209","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
Isolation, identification and optimization for tyrosinase production by banana peel waste for industrial application.
The study aimed to isolate, purify and optimise tyrosinase from banana peel waste for industrial use. Tyrosinase was extracted from banana peel using phosphate buffer. Purification initiated with centrifugation followed by ammonium sulphate precipitation. Further purification and characterisation was done through gel filtration. Bradford assay was used to determine the protein concentration. Enzyme activity of each sample was measured using tyrosinase activity assay. The pH and temperature optimisation of tyrosinase were also obtained. Results indicated that fractions obtained through ammonium sulphate precipitation at 70% saturation showed more activity than that of crude extract and 35% saturated fractions. Gel filtration column results showed that fraction number 17 &18 have maximum activity. Tyrosinase showed maximum activity at pH 7.0; 37 °C. Comparison between industrially purified and lab-isolated enzyme showed that both have similar optimum pH and temperature. It can be concluded that banana peel can be a source for synthesis of tyrosinase.
期刊介绍:
The aim of Natural Product Research is to publish important contributions in the field of natural product chemistry. The journal covers all aspects of research in the chemistry and biochemistry of naturally occurring compounds.
The communications include coverage of work on natural substances of land and sea and of plants, microbes and animals. Discussions of structure elucidation, synthesis and experimental biosynthesis of natural products as well as developments of methods in these areas are welcomed in the journal. Finally, research papers in fields on the chemistry-biology boundary, eg. fermentation chemistry, plant tissue culture investigations etc., are accepted into the journal.
Natural Product Research issues will be subtitled either ""Part A - Synthesis and Structure"" or ""Part B - Bioactive Natural Products"". for details on this , see the forthcoming articles section.
All manuscript submissions are subject to initial appraisal by the Editor, and, if found suitable for further consideration, to peer review by independent, anonymous expert referees. All peer review is single blind and submission is online via ScholarOne Manuscripts.