{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T03:49:51Z","timestamp":1785469791623,"version":"3.56.0"},"reference-count":41,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2021,2,25]],"date-time":"2021-02-25T00:00:00Z","timestamp":1614211200000},"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>The unique chemical, optical, and electrical characteristics of nanoparticles make their utilization highly successful in every field of biological sciences as compared to their bulk counterpart. These properties arise as a result of their miniature size, which provides them an excellent surface area-to-volume ratio, inner structure, and shape, and hence increases their surface characteristics. Therefore, this study was undertaken to engineer gold nanoparticles (AuNPs) for improving their catalytic activity and stability in biotechnological processes. The characterization of AuNPs was performed by XRD, UV spectra, and TEM. The synthesized AuNPs were surface-modified by polyvinyl alcohol (PVA) for binding the enzyme in excellent yield. The developed immobilized enzyme system (PVA-AuNPs-\u03b2-galactosidase) displayed pH optima at pH 7.0 and temperature optima at 40 \u00b0C. Moreover, the stability of PVA-AuNPs-\u03b2-galactosidase was significantly enhanced at wider pH and temperature ranges and at higher galactose concentrations, in contrast to the free enzyme. \u03b2-galactosidase bound to PVA-modified AuNPs exhibited greater operational activity, even after its sixth reuse. The developed nanosystem may prove useful in producing lactose-free dairy products for lactose-intolerant patients.<\/jats:p>","DOI":"10.3390\/molecules26051226","type":"journal-article","created":{"date-parts":[[2021,2,26]],"date-time":"2021-02-26T02:08:17Z","timestamp":1614305297000},"page":"1226","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Stabilization of \u03b2-Galactosidase on Modified Gold Nanoparticles: A Preliminary Biochemical Study to Obtain Lactose-Free Dairy Products for Lactose-Intolerant Individuals"],"prefix":"10.3390","volume":"26","author":[{"given":"Asim Muhammed","family":"Alshanberi","sequence":"first","affiliation":[{"name":"Department of Community Medicine and Pilgrims Health Care, Umm Alqura University, Makkah 24382, Saudi Arabia"},{"name":"Department of Biochemistry, School of Medicine, Batterjee Medical College for Sciences and Technology, Jeddah 21442, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rukhsana","family":"Satar","sequence":"additional","affiliation":[{"name":"Division of Biochemistry, Ibn Sina National College for Medical Studies, Jeddah 22421, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shakeel Ahmed","family":"Ansari","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, School of Medicine, Batterjee Medical College for Sciences and Technology, Jeddah 21442, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,2,25]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Rocchitta, G., Spanu, A., Babudieri, S., Latte, G., Madeddu, G., Galleri, G., Nuvoli, S., Bagella, P., Demartis, M.I., and Fiore, V. (2016). Enzyme biosensors for biomedical applications: Strategies for safeguarding analytical performances in biological fluids. Sensors, 16.","DOI":"10.3390\/s16060780"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"6437","DOI":"10.1039\/c3cs35506c","article-title":"Industrial use of immobilized enzymes","volume":"42","author":"Dicosimo","year":"2013","journal-title":"Chem. Soc. Rev."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1002\/bit.21570","article-title":"Three-dimensional immobilization of \u03b2-galactosidase on a silicon surface","volume":"99","author":"Betancor","year":"2008","journal-title":"Biotechnol. Bioeng."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1386","DOI":"10.1007\/s12010-009-8600-5","article-title":"Immobilization of \u03b2-galactosidase onto magnetic beads","volume":"160","author":"Zhang","year":"2010","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.molcatb.2011.02.016","article-title":"Immobilization of Kluyveromyces lactis \u03b2 galactosidase on concanavalin A layered aluminium oxide nanoparticles-its future aspects in biosensor applications","volume":"70","author":"Ansari","year":"2011","journal-title":"J. Mol. Cat. B Enz."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.molcatb.2009.12.010","article-title":"Lactose hydrolysis by \u03b2 galactosidase immobilized on concanavalin A-cellulose in batch and continuous mode","volume":"63","author":"Ansari","year":"2010","journal-title":"J. Mol. Cat. B Enz."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/j.enzmictec.2005.03.007","article-title":"Immobilization of tomato pectinase on Con A\u2013Seralose 4B by bioaffinity layering","volume":"37","author":"Sardar","year":"2005","journal-title":"Enz. Microb. Technol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1021\/bm701343m","article-title":"Novel dense CO2 technique for beta-galactosidase immobilization in polystyrene microchannels","volume":"9","author":"Ellis","year":"2008","journal-title":"Biomacromolecules"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.molcatb.2009.07.003","article-title":"Novel and efficient method for immobilization and stabilization of \u03b2-d-galactosidase by covalent attachment onto magnetic Fe3O4-chitosan nanoparticles","volume":"61","author":"Pan","year":"2009","journal-title":"J. Mol. Catal. B Enzym."},{"key":"ref_10","first-page":"768","article-title":"Design of immobilized enzyme biocatalysts: Drawbacks and opportunities","volume":"42","author":"Reis","year":"2019","journal-title":"Quim. Nov."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1007\/978-1-0716-0215-7_6","article-title":"Multi-point covalent immobilization of enzymes on supports activated with epoxy groups: Stabilization of industrial enzymes","volume":"2100","author":"Mateo","year":"2020","journal-title":"Meth. Mol. Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/j.fbp.2014.10.014","article-title":"Nanodiamonds as an effective and novel matrix for immobilizing \u03b2 galactosidase","volume":"95","author":"Ansari","year":"2015","journal-title":"Food Bioprod. Proc."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2885","DOI":"10.1002\/adsc.201100163","article-title":"Potential of different enzyme immobilization strategies to improve enzyme performance","volume":"353","author":"Rodrigues","year":"2011","journal-title":"Adv. Synth. Catal."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.biori.2017.01.004","article-title":"Support engineering: Relation between development of new supports for immobilization of lipases and their applications","volume":"1","author":"Cipolatti","year":"2017","journal-title":"Biotechnol. Res. Innov."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.molcatb.2013.10.019","article-title":"Current status and trends in enzymatic nanoimmobilization","volume":"99","author":"Cipolatti","year":"2014","journal-title":"J. Mol. Catal. B Enz."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"104675","DOI":"10.1039\/C6RA22047A","article-title":"Nanomaterials for biocatalyst immobilization\u2014State of the art and future trends","volume":"106","author":"Cipolatti","year":"2016","journal-title":"RSC Adv."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Mokhtar, N.M., Rahman, R.N.Z.R., Noor, N.D.M., Shariff, F.M., and Ali, M.S.M. (2020). The immobilization of lipases on porous support by adsorption and hydrophobic interaction method. Catalysts, 10.","DOI":"10.3390\/catal10070744"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"36","DOI":"10.3389\/fbioe.2020.00036","article-title":"Effects of Enzyme Loading and Immobilization Conditions on the Catalytic Features of Lipase From Pseudomonas fluorescens Immobilized on Octyl-Agarose Beads","volume":"8","author":"Rios","year":"2020","journal-title":"Front. Bioeng. Biotechnol."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Zdarta, J., Meyer, A.S., Jesionowski, T., and Pinelo, M. (2018). A General Overview of Support Materials for Enzyme Immobilization: Characteristics, Properties, Practical Utility. Catalysts, 8.","DOI":"10.3390\/catal8020092"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"An, J., Li, G., Zhang, Y., Zhang, T., Liu, X., Gao, F., Peng, M., He, Y., and Fan, H. (2020). Recent advances in enzyme-nanostructure biocatalysts with enhanced activity. Catalysts, 10.","DOI":"10.3390\/catal10030338"},{"key":"ref_21","first-page":"1","article-title":"A review on the classification, characterization, synthesis of nanoparticles and their application","volume":"263","author":"Ealias","year":"2017","journal-title":"IOP Conf. Ser. Mater. Sci. Eng."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"11109","DOI":"10.1039\/C8RA00052B","article-title":"Impact of nanoparticle surface modification on the mechanical properties of polystyrene-based nanocomposites","volume":"8","author":"Kockmann","year":"2018","journal-title":"RSC Adv."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1021\/la062042s","article-title":"Colloidal stabilization of nanoparticles in concentrated suspensions","volume":"23","author":"Studart","year":"2007","journal-title":"Langmuir"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.2174\/1568026615666150414144750","article-title":"Biomedical applications of gold nanoparticles","volume":"15","author":"Cabuzu","year":"2015","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1021\/acs.accounts.6b00506","article-title":"Surface modification of gold nanoparticles with small molecules for biochemical analysis","volume":"50","author":"Chen","year":"2017","journal-title":"Acc. Chem. Res."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/s13205-017-0645-5","article-title":"Sources of \u03b2-galactosidase and its applications in food industry","volume":"7","author":"Saqib","year":"2017","journal-title":"3 Biotech."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"258","DOI":"10.14720\/aas.2017.110.1.1","article-title":"Potential application of \u03b2-galactosidase in food science and nutrition","volume":"110","author":"Zibrat","year":"2017","journal-title":"Acta. Agric. Slov."},{"key":"ref_28","first-page":"34","article-title":"Gold nanoparticles in biology and medicine: Recent advances and prospects","volume":"3","author":"Dykman","year":"2011","journal-title":"Act. Nat."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"356","DOI":"10.12688\/f1000research.7595.1","article-title":"Nanoparticle-based antimicrobials: Surface functionality is critical","volume":"5","author":"Gupta","year":"2016","journal-title":"F1000Research"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"127863","DOI":"10.1016\/j.foodchem.2020.127863","article-title":"A simple and sensitive sensor for lactose based on cascade reactions in Au nanoclusters and enzymes co-encapsulated metal-organic frameworks","volume":"339","author":"Guo","year":"2021","journal-title":"Food Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1016\/j.biotechadv.2011.09.005","article-title":"Potential applications of enzymes immobilized on\/in nanoparticles: A review","volume":"30","author":"Ansari","year":"2012","journal-title":"Biotechnol. Adv."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"7006","DOI":"10.1021\/jp035972i","article-title":"Characterization of gold nanoparticles synthesized using sucrose by seeding formation in the solid phase and seeding growth in aqueous solution","volume":"108","author":"Qi","year":"2004","journal-title":"J. Phys. Chem. B"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1007\/s12291-013-0358-4","article-title":"Preparation and characterization of gold nanoparticles with amino acids, examination of their stability","volume":"29","author":"Zarabi","year":"2014","journal-title":"Ind. J. Clin. Biochem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.molcatb.2006.10.005","article-title":"Improving the stability of cellulase by immobilization on modified polyvinyl alcohol coated chitosan beads","volume":"45","author":"Dincer","year":"2007","journal-title":"J. Mol. Catal. B Enzym."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1007\/s00449-016-1560-6","article-title":"Elucidating the binding efficacy of \u03b2-galactosidase on graphene by docking approach and its potential application in galacto-oligosaccharide production","volume":"39","author":"Satar","year":"2016","journal-title":"Bioproc. Biosyst. Eng."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"33","DOI":"10.15171\/ijb.1261","article-title":"Stability improvement of immobilized \u03b1-amylase using nano pore zeolite","volume":"14","author":"Talebi","year":"2016","journal-title":"Iran. J. Biotech."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1007\/s12257-010-0070-7","article-title":"Effects of various inhibitors on \u03b2-galactosidase purified from the thermoacidophilic Alicyclobacillus acidocaldarius subsp. Rittmannii isolated from Antarctica","volume":"16","author":"Guven","year":"2011","journal-title":"Biotechnol. Bioproc. Eng."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1590\/0104-6632.20190361s20180135","article-title":"Biotechnological application of surface modified cerium oxide nanoparticles","volume":"36","author":"Ansari","year":"2019","journal-title":"Braz. J. Chem. Eng."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1021\/ed081p544A","article-title":"Color my nanoworld","volume":"81","author":"McFarland","year":"2004","journal-title":"J. Chem. Educ."},{"key":"ref_40","first-page":"1","article-title":"One-pot synthesis and surface modification of Fe3O4 nanoparticles using polyvinyl alcohol by coprecipitation and ultrasonication methods","volume":"299","author":"Nugraha","year":"2018","journal-title":"IOP Conf. Ser. Mat. Sci. Eng."},{"key":"ref_41","first-page":"429","article-title":"Utility of functionalized agarose nanoparticles in hydrolyzing lactose in batch reactors for dairy industries","volume":"41","author":"Ansari","year":"2018","journal-title":"Quim. Nov."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/26\/5\/1226\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T05:28:37Z","timestamp":1760160517000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/26\/5\/1226"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,2,25]]},"references-count":41,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2021,3]]}},"alternative-id":["molecules26051226"],"URL":"https:\/\/doi.org\/10.3390\/molecules26051226","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,2,25]]}}}