{"title":"羧基功能化多壁碳纳米管对无花果曲霉鞣酶的吸附研究","authors":"Matthew Alias, C. Ong, Annuar Mohamad","doi":"10.2298/jsc221121009a","DOIUrl":null,"url":null,"abstract":"The immobilization of cross-linked tannase onto carboxyl-functionalized multi-walled carbon nanotubes (MWCNT?COOH) was achieved via physical adsorption. Glutaraldehyde was used to cross-link the enzyme molecules. Spectroscopic and morphological characterizations of the enzyme-nanotubes composite were carried out, which authenticated the successful adsorption event. Enzyme composite is proven equal to-, or even superior than free tannase, in terms of catalytic activities and stabilities, when measured under different thermal-, pH-, and recycling conditions. Whilst both free- and immobilized tannase preparations exhibited optimum catalysis at pH 5.0 and 35?C, tannase-nanotubes composite possesses better thermal stability. The immobilized preparation retained 75% of its initial catalytic activity following ten consecutives use. The study demonstrated a facile method to produce catalytically-efficient nanobiocatalyst composite for biotechnological applications.","PeriodicalId":17489,"journal":{"name":"Journal of The Serbian Chemical Society","volume":"1 1","pages":""},"PeriodicalIF":1.0000,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Adsorption of Tannase from Aspergillus ficuum to carboxyl-functionalized multi-walled carbon nanotubes\",\"authors\":\"Matthew Alias, C. Ong, Annuar Mohamad\",\"doi\":\"10.2298/jsc221121009a\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The immobilization of cross-linked tannase onto carboxyl-functionalized multi-walled carbon nanotubes (MWCNT?COOH) was achieved via physical adsorption. Glutaraldehyde was used to cross-link the enzyme molecules. Spectroscopic and morphological characterizations of the enzyme-nanotubes composite were carried out, which authenticated the successful adsorption event. Enzyme composite is proven equal to-, or even superior than free tannase, in terms of catalytic activities and stabilities, when measured under different thermal-, pH-, and recycling conditions. Whilst both free- and immobilized tannase preparations exhibited optimum catalysis at pH 5.0 and 35?C, tannase-nanotubes composite possesses better thermal stability. The immobilized preparation retained 75% of its initial catalytic activity following ten consecutives use. The study demonstrated a facile method to produce catalytically-efficient nanobiocatalyst composite for biotechnological applications.\",\"PeriodicalId\":17489,\"journal\":{\"name\":\"Journal of The Serbian Chemical Society\",\"volume\":\"1 1\",\"pages\":\"\"},\"PeriodicalIF\":1.0000,\"publicationDate\":\"2023-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of The Serbian Chemical Society\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.2298/jsc221121009a\",\"RegionNum\":4,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of The Serbian Chemical Society","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.2298/jsc221121009a","RegionNum":4,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Adsorption of Tannase from Aspergillus ficuum to carboxyl-functionalized multi-walled carbon nanotubes
The immobilization of cross-linked tannase onto carboxyl-functionalized multi-walled carbon nanotubes (MWCNT?COOH) was achieved via physical adsorption. Glutaraldehyde was used to cross-link the enzyme molecules. Spectroscopic and morphological characterizations of the enzyme-nanotubes composite were carried out, which authenticated the successful adsorption event. Enzyme composite is proven equal to-, or even superior than free tannase, in terms of catalytic activities and stabilities, when measured under different thermal-, pH-, and recycling conditions. Whilst both free- and immobilized tannase preparations exhibited optimum catalysis at pH 5.0 and 35?C, tannase-nanotubes composite possesses better thermal stability. The immobilized preparation retained 75% of its initial catalytic activity following ten consecutives use. The study demonstrated a facile method to produce catalytically-efficient nanobiocatalyst composite for biotechnological applications.
期刊介绍:
The Journal of the Serbian Chemical Society -JSCS (formerly Glasnik Hemijskog društva Beograd) publishes articles original papers that have not been published previously, from the fields of fundamental and applied chemistry:
Theoretical Chemistry, Organic Chemistry, Biochemistry and Biotechnology, Food Chemistry, Technology and Engineering, Inorganic Chemistry, Polymers, Analytical Chemistry, Physical Chemistry, Spectroscopy, Electrochemistry, Thermodynamics, Chemical Engineering, Textile Engineering, Materials, Ceramics, Metallurgy, Geochemistry, Environmental Chemistry, History of and Education in Chemistry.