{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T17:48:44Z","timestamp":1790358524028,"version":"4.1.0"},"reference-count":32,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2023,1,3]],"date-time":"2023-01-03T00:00:00Z","timestamp":1672704000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>To increase its operational stability and ongoing reusability, B. subtilis pectinase was immobilized on iron oxide nanocarrier. Through co-precipitation, magnetic iron oxide nanoparticles were synthesized. Scanning electron microscopy (SEM) and energy dispersive electron microscopy (EDEX) were used to analyze the nanoparticles. Pectinase was immobilized using glutaraldehyde as a crosslinking agent on iron oxide nanocarrier. In comparison to free pectinase, immobilized pectinase demonstrated higher enzymatic activity at a variety of temperatures and pH levels. Immobilization also boosted pectinase\u2019s catalytic stability. After 120 h of pre-incubation at 50 \u00b0C, immobilized pectinase maintained more than 90% of its initial activity due to the iron oxide nanocarrier, which improved the thermal stability of pectinase at various temperatures. Following 15 repetitions of enzymatic reactions, immobilized pectinase still exhibited 90% of its initial activity. According to the results, pectinase\u2019s catalytic capabilities were enhanced by its immobilization on iron oxide nanocarrier, making it economically suitable for industrial use.<\/jats:p>","DOI":"10.3390\/molecules28010404","type":"journal-article","created":{"date-parts":[[2023,1,3]],"date-time":"2023-01-03T02:51:39Z","timestamp":1672714299000},"page":"404","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Development of Pectinase Based Nanocatalyst by Immobilization of Pectinase on Magnetic Iron Oxide Nanoparticles Using Glutaraldehyde as Crosslinking Agent"],"prefix":"10.3390","volume":"28","author":[{"given":"Tayyaba","family":"Behram","sequence":"first","affiliation":[{"name":"Department of Biotechnology, Shaheed Benazir Bhutto University, Sheringal Dir Upper 18000, Pakistan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sidra","family":"Pervez","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Shaheed Benazir Bhutto Women University, Peshawar 25000, Pakistan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4526-9380","authenticated-orcid":false,"given":"Muhammad Asif","family":"Nawaz","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Shaheed Benazir Bhutto University, Sheringal Dir Upper 18000, Pakistan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4449-6525","authenticated-orcid":false,"given":"Shujaat","family":"Ahmad","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, Shaheed Benazir Bhutto University, Sheringal Dir Upper 18000, Pakistan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amin Ullah","family":"Jan","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Shaheed Benazir Bhutto University, Sheringal Dir Upper 18000, Pakistan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haneef Ur","family":"Rehman","sequence":"additional","affiliation":[{"name":"Department of Natural and Basic Sciences, University of Turbat, Kech, Turbat 92600, Pakistan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0173-0892","authenticated-orcid":false,"given":"Shahbaz","family":"Ahmad","sequence":"additional","affiliation":[{"name":"Department of Biological Science and Engineering, School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing 100083, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7347-1127","authenticated-orcid":false,"given":"Nasir Mehmood","family":"Khan","sequence":"additional","affiliation":[{"name":"Department of Agriculture, Shaheed Benazir Bhutto University, Sheringal Dir Upper 18000, Pakistan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5730-7730","authenticated-orcid":false,"given":"Farman Ali","family":"Khan","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Shaheed Benazir Bhutto University, Sheringal Dir Upper 18000, Pakistan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,1,3]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.biortech.2003.05.003","article-title":"Production, characterization and application of a thermostable polygalacturonase of a thermophilic mould Sporotrichum thermophile apinis","volume":"94","author":"Kaur","year":"2004","journal-title":"Bioresour. Technol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1007\/s00253-002-1061-1","article-title":"Microbial alkaline pectinase and their industrial application","volume":"59","author":"Hoondal","year":"2002","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2931","DOI":"10.1016\/j.procbio.2005.03.026","article-title":"Microbial pectinolytic enzymes: A review","volume":"40","author":"Jayani","year":"2005","journal-title":"Process Biochem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1016\/j.foodchem.2013.01.069","article-title":"Degradation of complex carbohydrate: Immobilization of pectinase from Bacillus licheniformis KIBGE-IB21 using calcium alginate as a support","volume":"139","author":"Rehman","year":"2013","journal-title":"Food Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1016\/j.carbpol.2013.11.073","article-title":"Immobilization of pectin degrading enzyme from Bacillus licheniformis KIBGE IB-21 using agar-agar as a support","volume":"102","author":"Rehman","year":"2014","journal-title":"Carbohydr. Polym."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/j.bcab.2014.09.003","article-title":"Immobilization of pectinase from Bacillus licheniformis KIBGE-IB21 on chitosan beads for continuous degradation of pectin polymers","volume":"3","author":"Rehman","year":"2014","journal-title":"Biocatal. Agri. Biotechnol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1002\/adsc.200700082","article-title":"Enzyme immobilization: The quest for optimum performance","volume":"349","author":"Sheldon","year":"2007","journal-title":"Adv. Syn. Catal."},{"key":"ref_8","first-page":"1","article-title":"Pectinase: Immobilization and applications. A review","volume":"6","author":"Rehman","year":"2021","journal-title":"Trends Pept. Protein Sci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1016\/j.enzmictec.2006.10.027","article-title":"The silica-coated chitosan particle from a layer-by-layer approach for pectinase immobilization","volume":"40","author":"Lei","year":"2007","journal-title":"Enzyme Microbial. Technol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.foodchem.2008.01.012","article-title":"Immobilization and stabilization of pectinase by multipoint attachment onto an activated agar-gel support","volume":"109","author":"Li","year":"2008","journal-title":"Food Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1007\/3-540-68116-7_4","article-title":"Immobilized Enzymes: Methods and Applications","volume":"Volume 200","author":"Tischer","year":"1999","journal-title":"Biocatalysis-from Discovery to Application"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"e04578","DOI":"10.1016\/j.heliyon.2020.e04578","article-title":"Encapsulation of pectinase within polyacrylamide gel: Characterization of its catalytic properties for continuous industrial uses","volume":"6","author":"Rehman","year":"2020","journal-title":"Heliyon"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Mohammadi, Z.B., Zhang, F., Kharazmi, M.S., and Jafari, S.M. (2022). Nano-biocatalysts for food applications; immobilized enzymes within different nanostructures. Crit. Rev. Food Sci. Nutr., 1\u201319.","DOI":"10.1080\/10408398.2022.2092719"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"112602","DOI":"10.1016\/j.colsurfb.2022.112602","article-title":"Design of Composite Nanosupports and applications thereof in Enzyme Immobilization: A Review","volume":"217","author":"Lu","year":"2022","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"107738","DOI":"10.1016\/j.biotechadv.2021.107738","article-title":"Trends in the development of innovative nanobiocatalysts and their application in biocatalytic transformations","volume":"51","author":"Gkantzou","year":"2021","journal-title":"Biotechnol. Adv."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"110607","DOI":"10.1016\/j.mcat.2019.110607","article-title":"Industrial applications of immobilized enzymes. A review","volume":"479","author":"Basso","year":"2019","journal-title":"Mol. Catal."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1007\/s10529-015-1977-z","article-title":"Application of magnetic nanoparticles in smart enzyme immobilization","volume":"38","author":"Vaghari","year":"2016","journal-title":"Biotechnol. Lett."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2530","DOI":"10.1016\/j.ijbiomac.2018.09.025","article-title":"Magnetic nanoparticles as versatile carriers for enzymes immobilization: A review","volume":"120","author":"Bilal","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"233","DOI":"10.3389\/fbioe.2019.00233","article-title":"Magnetic separation in bioprocessing beyond the analytical scale: From biotechnology to the food industry","volume":"7","author":"Schwaminger","year":"2019","journal-title":"Front. Bioeng. Biotechnol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1016\/j.carbpol.2012.10.061","article-title":"Evaluation of free and immobilized Aspergillus niger NRC1ami pectinase applicable in industrial processes","volume":"92","author":"Esawy","year":"2013","journal-title":"Carbohydr. Polym."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1007\/s00449-006-0073-0","article-title":"Immobilization of urease by using chitosan-alginate and poly(acrylamide-co-acrylic acid)\/kappa-carrageenan supports","volume":"29","author":"Kara","year":"2006","journal-title":"Bioprocess Biosyst. Eng."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molcatb.2013.03.010","article-title":"Electrostatic immobilization of pectinase on negatively charged AOT-Fe3O4 nanoparticles","volume":"93","author":"Bahrami","year":"2013","journal-title":"J. Mol. Catal."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.micromeso.2008.03.030","article-title":"Structural features of penicillin acylase adsorption on APTES functionalized SBA-15","volume":"116","author":"Shah","year":"2008","journal-title":"Microporous Mesoporous Mat."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1021\/ja01318a036","article-title":"The determination of enzyme dissociation constants","volume":"56","author":"Lineweaver","year":"1934","journal-title":"J. Am. Chem. Soc."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"2273","DOI":"10.1016\/j.msec.2013.01.050","article-title":"Fabrication, characterization and application of pectin degrading Fe3O4-SiO2 nanobiocatalyst","volume":"33","author":"Seenuvasan","year":"2013","journal-title":"Mater. Sci. Eng. C"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1021\/bp050334y","article-title":"Characteristics of a mesoporous silicate immobilized trypsin bioreactor in organic media","volume":"22","author":"Goradia","year":"2006","journal-title":"Biotechnol. Progress"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.bej.2012.06.002","article-title":"Direct binding glucoamylase onto carboxyl-functioned magnetic nanoparticles","volume":"67","author":"Chen","year":"2012","journal-title":"Biochem. Eng. J."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.desal.2009.11.043","article-title":"Adsorption of Cu(II) from aqueous solution by using modified Fe3O4 magnetic nano-particles","volume":"254","author":"Ozmen","year":"2010","journal-title":"Desalination"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"83856","DOI":"10.1039\/C6RA17167B","article-title":"Immobilization of soybean peroxidase on silica-coated magnetic particles: A magnetically recoverable biocatalyst for pollutant removal","volume":"87","author":"Silva","year":"2016","journal-title":"RSC Adv."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"102805","DOI":"10.1016\/j.jece.2018.11.049","article-title":"Development of peroxidase enzyme immobilized magnetic nanoparticles for bioremediation of textile wastewater dye","volume":"7","author":"Darwesh","year":"2019","journal-title":"J. Environ. Chem. Eng."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1021\/ac60147a030","article-title":"Use of dinitrosalicylic acid reagent for determination of reducing sugars","volume":"31","author":"Miller","year":"1959","journal-title":"Analyt. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","article-title":"Protein measurement with the Folin phenol reagent","volume":"193","author":"Lowry","year":"1951","journal-title":"J. Biol. Chem."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/28\/1\/404\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T17:56:58Z","timestamp":1760119018000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/28\/1\/404"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,1,3]]},"references-count":32,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2023,1]]}},"alternative-id":["molecules28010404"],"URL":"https:\/\/doi.org\/10.3390\/molecules28010404","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,1,3]]}}}