{"title":"Improved Stability of Aspergillus oryzae α-Amylase Immobilized on Polyaniline Tin Oxide Nanocomposites","authors":"Mohd Jahir Khan, Abrar Ahmad","doi":"10.2174/0113852728295467240219051245","DOIUrl":null,"url":null,"abstract":": In the present study, an immobilization support, Polyaniline tin oxide nanocomposite (PANI-SnO2- NC) was synthesized by in situ polymerization of aniline and ammonium peroxydisulphate. The prepared nanocomposite was characterized by various state-of-the-art techniques. The average size of native SnO2-NPs and PANI-SnO2-NC was 65±19 nm and 93±15 nm, respectively. An important industrial enzyme, α-amylase from Aspergillus oryzae was immobilized on PANI-SnO2-NC, which retained 87% enzyme activity. The improved stability of the immobilized enzyme was noticed against pH and temperature, as it retained 65% activity at 60 °C while the free enzyme exhibited 41% activity under similar experimental conditions. Moreover, PANI-SnO2- NC-immobilized α-amylase produced starch (26.42 mg mL–1) more efficiently than free enzyme (20.90 mg mL– 1) after 8 h in batch hydrolysis. PANI-SnO2-NC-bound α-amylase exhibited 54% activity after eight repeated uses. Molecular docking analysis of α-amylase with PANI suggested the ligand binding site to be located quite far away from the active site of the enzyme.","PeriodicalId":10926,"journal":{"name":"Current Organic Chemistry","volume":null,"pages":null},"PeriodicalIF":1.7000,"publicationDate":"2024-04-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Organic Chemistry","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.2174/0113852728295467240219051245","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, ORGANIC","Score":null,"Total":0}
引用次数: 0
Abstract
: In the present study, an immobilization support, Polyaniline tin oxide nanocomposite (PANI-SnO2- NC) was synthesized by in situ polymerization of aniline and ammonium peroxydisulphate. The prepared nanocomposite was characterized by various state-of-the-art techniques. The average size of native SnO2-NPs and PANI-SnO2-NC was 65±19 nm and 93±15 nm, respectively. An important industrial enzyme, α-amylase from Aspergillus oryzae was immobilized on PANI-SnO2-NC, which retained 87% enzyme activity. The improved stability of the immobilized enzyme was noticed against pH and temperature, as it retained 65% activity at 60 °C while the free enzyme exhibited 41% activity under similar experimental conditions. Moreover, PANI-SnO2- NC-immobilized α-amylase produced starch (26.42 mg mL–1) more efficiently than free enzyme (20.90 mg mL– 1) after 8 h in batch hydrolysis. PANI-SnO2-NC-bound α-amylase exhibited 54% activity after eight repeated uses. Molecular docking analysis of α-amylase with PANI suggested the ligand binding site to be located quite far away from the active site of the enzyme.
期刊介绍:
Current Organic Chemistry aims to provide in-depth/mini reviews on the current progress in various fields related to organic chemistry including bioorganic chemistry, organo-metallic chemistry, asymmetric synthesis, heterocyclic chemistry, natural product chemistry, catalytic and green chemistry, suitable aspects of medicinal chemistry and polymer chemistry, as well as analytical methods in organic chemistry. The frontier reviews provide the current state of knowledge in these fields and are written by chosen experts who are internationally known for their eminent research contributions. The Journal also accepts high quality research papers focusing on hot topics, highlights and letters besides thematic issues in these fields. Current Organic Chemistry should prove to be of great interest to organic chemists in academia and industry, who wish to keep abreast with recent developments in key fields of organic chemistry.