{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T18:33:22Z","timestamp":1784745202064,"version":"3.55.0"},"reference-count":57,"publisher":"Public Library of Science (PLoS)","issue":"7","license":[{"start":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T00:00:00Z","timestamp":1784678400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS One"],"abstract":"<jats:p>\n                    Palm weevil (\n                    <jats:italic>Rhynchophorus palmarum<\/jats:italic>\n                    L.) is a significant pest that has been identified as a threat to palm trees in tropical regions. Beyond its agricultural impact, its digestive system represents a promising source of biocatalysts. The present study investigates the catalytic activity of\n                    <jats:italic>\u03b2<\/jats:italic>\n                    -galactosidase extracted from the digestive juice of\n                    <jats:italic>R. palmarum<\/jats:italic>\n                    larvae.\n                    <jats:italic>o<\/jats:italic>\n                    -nitrophenyl-\n                    <jats:italic>\u03b2<\/jats:italic>\n                    -D-galactopyranoside (\n                    <jats:italic>o<\/jats:italic>\n                    NPG) was utilized as the substrate in this investigation. The purified enzyme exhibited optimal activity at 330.0\u2009\u00b1\u20091.2 K and pH\u2009=\u20095.0\u2009\u00b1\u20090.1, as determined by empirical and mechanistic models. The activation energy (E\n                    <jats:sub>a<\/jats:sub>\n                    ) was estimated at 56.3\u2009\u00b1\u20099 kJ mol\n                    <jats:sup>-1<\/jats:sup>\n                    using mechanistic models. Furthermore, the pK values for the enzyme-substrate complex were determined to be 4.0\u2009\u00b1\u20090.1 for the nucleophile and 6.2\u2009\u00b1\u20090.2 for the proton donor, which provides insight into the catalytic residues. Kinetic analysis through nonlinear regression yielded a catalytic constant (k\n                    <jats:sub>cat<\/jats:sub>\n                    ) of 4.9\u2009\u00d7\u200910\n                    <jats:sup>3<\/jats:sup>\n                    s\n                    <jats:sup>-1<\/jats:sup>\n                    with V\n                    <jats:sub>max<\/jats:sub>\n                    and K\n                    <jats:sub>m<\/jats:sub>\n                    values of 49\u2009\u00b1\u20092 U mg\n                    <jats:sup>-1<\/jats:sup>\n                    and 0.77\u2009\u00b1\u20090.08 mM, respectively. The results obtained provide novel insights into the physicochemical properties of this enzyme. The findings of this study demonstrated that the insect digestive system is a promising and largely untapped source of robust\n                    <jats:italic>\u03b2<\/jats:italic>\n                    -galactosidases with considerable potential for industrial biocatalytic applications.\n                  <\/jats:p>","DOI":"10.1371\/journal.pone.0354469","type":"journal-article","created":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T17:41:32Z","timestamp":1784742092000},"page":"e0354469","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":0,"title":["Kinetic and physicochemical modeling of \u03b2-galactosidase from Rhynchophorus palmarum larvae"],"prefix":"10.1371","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8645-1018","authenticated-orcid":true,"given":"Sobamfou Marius","family":"Kambir\u00e9","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mankambou Jacques","family":"Gnanwa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Boa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"N\u2019guessan Eug\u00e8ne Jean Parfait","family":"Kouadio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bonito Aristide","family":"Karamoko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2026,7,22]]},"reference":[{"key":"pone.0354469.ref001","first-page":"022046","article-title":"Mini review on role of \u03b2-galactosidase in lactose intolerance","volume":"263","author":"A Nivetha","year":"2017","journal-title":"IOP Conf Ser: Mater Sci Eng"},{"issue":"1","key":"pone.0354469.ref002","doi-asserted-by":"crossref","first-page":"41","DOI":"10.3109\/07388550903330497","article-title":"Beta galactosidases and their potential applications: a review","volume":"30","author":"Q Husain","year":"2010","journal-title":"Crit Rev Biotechnol"},{"issue":"4","key":"pone.0354469.ref003","doi-asserted-by":"crossref","first-page":"307","DOI":"10.3109\/07388551.2013.794124","article-title":"Biotechnological potential of microbial \u03b1-galactosidases","volume":"34","author":"P Katrolia","year":"2014","journal-title":"Crit Rev Biotechnol"},{"issue":"3","key":"pone.0354469.ref004","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.yrtph.2004.07.011","article-title":"Toxicity evaluation of a beta-galactosidase preparation produced by Penicillium multicolor","volume":"40","author":"MT Flood","year":"2004","journal-title":"Regul Toxicol Pharmacol"},{"issue":"8","key":"pone.0354469.ref005","doi-asserted-by":"crossref","first-page":"4056","DOI":"10.1039\/C8FO00555A","article-title":"Lactose malabsorption and intolerance: a review","volume":"9","author":"S Ugidos-Rodr\u00edguez","year":"2018","journal-title":"Food Funct"},{"issue":"2","key":"pone.0354469.ref006","doi-asserted-by":"crossref","first-page":"85","DOI":"10.17221\/19\/2011-PPS","article-title":"Biochemical characterisation of \u03b1- and \u03b2-glucosidases and \u03b1- and \u03b2-galactosidases from red palm weevil, Rhynchophorus ferrugineus (Olivier) (Col.: Curculionide)","volume":"48","author":"NS Riseh","year":"2012","journal-title":"Plant Prot Sci"},{"key":"pone.0354469.ref007","doi-asserted-by":"crossref","first-page":"705","DOI":"10.2298\/ABS1103705S","article-title":"Biochemical characterization of digestive carbohydrases from Xanthogaleruca luteola and inhibition of its \u03b1-amylase by inhibitors extracted from the common bean","volume":"63","author":"M Sharifi","year":"2011","journal-title":"Arch Biol Sci"},{"issue":"3","key":"pone.0354469.ref008","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1093\/jee\/56.3.375","article-title":"The Role of the Palm Weevil, Rhynchophorus palmarum, as a Vector of Red Ring Disease of Coconuts. 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Results of Preliminary Investigations1","volume":"56","author":"EAC Hagley","year":"1963","journal-title":"Journal of Economic Entomology"},{"issue":"3","key":"pone.0354469.ref009","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1653\/0015-4040(2002)085[0507:CORRDB]2.0.CO;2","article-title":"Control of red ring disease by mass trapping of rhynchophorus palmarum (Coleoptera: Curculionidae)","volume":"85","author":"AC Oehlschlager","year":"2002","journal-title":"Florida Entomologist"},{"issue":"2","key":"pone.0354469.ref010","doi-asserted-by":"crossref","first-page":"185","DOI":"10.14411\/eje.2009.022","article-title":"Purification and characterization of a novel thermoacidophilic and thermostable \u03b1-mannosidase from the digestive fluid of oil palm weevil Rhynchophorus palmarum (Coleoptera: Curculionidae) larvae","volume":"106","author":"M B\u00e9dikou","year":"2009","journal-title":"Eur J Entomol"},{"issue":"4","key":"pone.0354469.ref011","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1111\/j.1479-8298.2007.00232.x","article-title":"Biochemical characterization of a strictly specific beta\u2010galactosidase from the digestive juice of the palm weevil Rhynchophorus palmarum larvae","volume":"10","author":"Dya Yapi","year":"2007","journal-title":"Entomological Science"},{"key":"pone.0354469.ref012","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1673\/031.009.0401","article-title":"Purification and biochemical characterization of a specific beta-glucosidase from the digestive fluid of larvae of the palm weevil, Rhynchophorus palmarum","volume":"9","author":"D Yapi Assoi Yapi","year":"2009","journal-title":"J Insect Sci"},{"issue":"10","key":"pone.0354469.ref013","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1016\/j.tibs.2010.05.001","article-title":"A new understanding of how temperature affects the catalytic activity of enzymes","volume":"35","author":"RM Daniel","year":"2010","journal-title":"Trends Biochem Sci"},{"key":"pone.0354469.ref014","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/S0968-0004(01)01894-1","article-title":"Erratum","volume":"26","author":"RM Daniel","year":"2001","journal-title":"Trends in Biochemical Sciences"},{"issue":"3","key":"pone.0354469.ref015","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/S0141-0229(02)00105-9","article-title":"Temperature optima of enzymes: sifting fact from fiction","volume":"31","author":"PR Patnaik","year":"2002","journal-title":"Enzyme and Microbial Technology"},{"issue":"1","key":"pone.0354469.ref016","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":"OH Lowry","year":"1951","journal-title":"J Biol Chem"},{"key":"pone.0354469.ref017","doi-asserted-by":"crossref","first-page":"309","DOI":"10.3354\/meps134309","article-title":"Quantifying the short-term temperature effect on light-saturated photosynthesis of intertidal microphytobenthos","volume":"134","author":"G Blanchard","year":"1996","journal-title":"Mar Ecol Prog Ser"},{"issue":"8","key":"pone.0354469.ref018","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1007\/s00449-016-1596-7","article-title":"A new method to determine optimum temperature and activation energies for enzymatic reactions","volume":"39","author":"M Wojcik","year":"2016","journal-title":"Bioprocess Biosyst Eng"},{"key":"pone.0354469.ref019","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.ecolmodel.2006.07.012","article-title":"A peaked function for modeling temperature dependence of plant productivity","volume":"200","author":"GA Alexandrov","year":"2007","journal-title":"Ecological Modelling"},{"key":"pone.0354469.ref020","doi-asserted-by":"crossref","first-page":"106611","DOI":"10.1016\/j.bpc.2021.106611","article-title":"Modeling of enzymatic activity of free \u03b2-glucosidase from palm weevil, Rhynchophorus palmarum Linn. (Coleoptera: Curculionidae) larvae: Effects of pH and temperature","volume":"276","author":"MS Kambir\u00e9","year":"2021","journal-title":"Biophys Chem"},{"key":"pone.0354469.ref021","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1128\/aem.61.2.610-616.1995","article-title":"Convenient Model To Describe the Combined Effects of Temperature and pH on Microbial Growth","volume":"61","author":"L Rosso","year":"1995","journal-title":"Appl. Environ. Microbiol"},{"issue":"4","key":"pone.0354469.ref022","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1006\/jtbi.1993.1099","article-title":"An unexpected correlation between cardinal temperatures of microbial growth highlighted by a new model","volume":"162","author":"L Rosso","year":"1993","journal-title":"J Theor Biol"},{"key":"pone.0354469.ref023","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.pisc.2014.02.005","article-title":"Enzyme assays","volume":"1","author":"H Bisswanger","year":"2014","journal-title":"Perspectives in Science"},{"issue":"3","key":"pone.0354469.ref024","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1007\/s00253-016-7833-9","article-title":"Eliminating hydrolytic activity without affecting the transglycosylation of a GH1 \u03b2-glucosidase","volume":"101","author":"P Lundemo","year":"2017","journal-title":"Appl Microbiol Biotechnol"},{"issue":"1","key":"pone.0354469.ref025","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.enzmictec.2003.07.004","article-title":"Kinetic models of activity for \u03b2-galactosidases: influence of pH, ionic concentration and temperature","volume":"34","author":"E Jurado","year":"2004","journal-title":"Enzyme and Microbial Technology"},{"key":"pone.0354469.ref026","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.ijfoodmicro.2014.06.014","article-title":"A model for the effect of pH on the growth of chalk yeasts","volume":"186","author":"P Dantigny","year":"2014","journal-title":"Int J Food Microbiol"},{"key":"pone.0354469.ref027","first-page":"125","article-title":"Biochemical characterization of glucosidases and galactosidases from Rosaceae ranch borer, Oosphranteria coerulescens redt. (Col.: Cerambycidae)","volume":"49","author":"N Aghaali","year":"2012","journal-title":"Romanian Journal of Biochemistry"},{"issue":"8","key":"pone.0354469.ref028","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1016\/0020-1790(87)90089-8","article-title":"Purification and characterization of \u03b2-galactosidase-1 from Drosophila melanogaster","volume":"17","author":"TR Fuerst","year":"1987","journal-title":"Insect Biochemistry"},{"key":"pone.0354469.ref029","article-title":"Enzyme kinetics: principles and methods for determining catalytic parameters","author":"H Bisswanger","year":"2017","journal-title":"Perspectives in Science"},{"issue":"12","key":"pone.0354469.ref030","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1021\/acs.biochem.5b01094","article-title":"On the Temperature Dependence of Enzyme-Catalyzed Rates","volume":"55","author":"VL Arcus","year":"2016","journal-title":"Biochemistry"},{"key":"pone.0354469.ref031","doi-asserted-by":"crossref","first-page":"152774","DOI":"10.1016\/j.ijbiomac.2026.152774","article-title":"Enhanced production, activity and deregulation of \u03b2-galactosidase in a new mutant strain Bifidobacterium longum BIM B-813 D: Characterization and industrial potential","volume":"369","author":"A \u041c\u043erozova","year":"2026","journal-title":"Int J Biol Macromol"},{"issue":"3","key":"pone.0354469.ref032","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/j.jbiosc.2015.01.015","article-title":"Novel acidophilic \u03b2-galactosidase with high activity at extremely acidic pH region from Teratosphaeria acidotherma AIU BGA-1","volume":"120","author":"S Chiba","year":"2015","journal-title":"J Biosci Bioeng"},{"issue":"5","key":"pone.0354469.ref033","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1016\/j.procbio.2014.02.008","article-title":"Cloning, purification and characterization of a thermostable \u03b2-galactosidase from Thermotoga naphthophila RUK-10","volume":"49","author":"F Kong","year":"2014","journal-title":"Process Biochemistry"},{"issue":"3","key":"pone.0354469.ref034","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.jbiosc.2013.03.012","article-title":"Characterization of new \u03b2-galactosidase from acidophilic fungus, Teratosphaeria acidotherma AIU BGA-1","volume":"116","author":"K Isobe","year":"2013","journal-title":"J Biosci Bioeng"},{"issue":"5","key":"pone.0354469.ref035","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.3168\/jds.2007-617","article-title":"Production, purification, and characterization of a potential thermostable galactosidase for milk lactose hydrolysis from Bacillus stearothermophilus","volume":"91","author":"W Chen","year":"2008","journal-title":"J Dairy Sci"},{"issue":"6","key":"pone.0354469.ref036","doi-asserted-by":"crossref","first-page":"954","DOI":"10.1016\/j.procbio.2010.02.025","article-title":"Purification and characterization of extracellular \u03b2-galactosidase from the psychrotolerant yeast Guehomyces pullulans 17-1 isolated from sea sediment in Antarctica","volume":"45","author":"C Song","year":"2010","journal-title":"Process Biochemistry"},{"issue":"9","key":"pone.0354469.ref037","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1016\/S0969-2126(01)00220-9","article-title":"Structures and mechanisms of glycosyl hydrolases","volume":"3","author":"G Davies","year":"1995","journal-title":"Structure"},{"issue":"6","key":"pone.0354469.ref038","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1016\/0959-440X(94)90271-2","article-title":"Mechanisms of enzymatic glycoside hydrolysis","volume":"4","author":"JD McCarter","year":"1994","journal-title":"Curr Opin Struct Biol"},{"issue":"13","key":"pone.0354469.ref039","doi-asserted-by":"crossref","first-page":"5281","DOI":"10.1007\/s00253-021-11423-7","article-title":"Challenges and perspectives of the \u03b2-galactosidase enzyme","volume":"105","author":"BIS Damin","year":"2021","journal-title":"Appl Microbiol Biotechnol"},{"issue":"12","key":"pone.0354469.ref040","doi-asserted-by":"crossref","first-page":"8193","DOI":"10.3168\/jds.2023-23392","article-title":"Invited review: Properties of \u03b2-galactosidases derived from Lactobacillaceae species and their capacity for galacto-oligosaccharide production","volume":"106","author":"S Ruiz-Ram\u00edrez","year":"2023","journal-title":"J Dairy Sci"},{"issue":"5","key":"pone.0354469.ref041","doi-asserted-by":"crossref","DOI":"10.1111\/jfbc.12564","article-title":"\u03b2-galactosidase: Biotechnological applications in food processing","volume":"42","author":"JR Xavier","year":"2018","journal-title":"J Food Biochem"},{"issue":"3","key":"pone.0354469.ref042","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1111\/1471-0307.13098","article-title":"\u03b2\u2010Galactosidase: Insights into source variability, genetic engineering, immobilisation and diverse applications in food, industry and medicine","volume":"77","author":"Y Zhou","year":"2024","journal-title":"Int J of Dairy Tech"},{"issue":"12","key":"pone.0354469.ref043","doi-asserted-by":"crossref","first-page":"1907","DOI":"10.1016\/j.jinsphys.2010.08.013","article-title":"Influence of iridoid glycoside containing host plants on midgut \u03b2-glucosidase activity in a polyphagous caterpillar, Spilosoma virginica Fabricius (Arctiidae)","volume":"56","author":"H Pankoke","year":"2010","journal-title":"J Insect Physiol"},{"issue":"3","key":"pone.0354469.ref044","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.crvi.2009.12.011","article-title":"Partial biochemical characterization of alpha- and beta-glucosidases of lesser mulberry pyralid, Glyphodes pyloalis Walker (Lep.: Pyralidae)","volume":"333","author":"M Ghadamyari","year":"2010","journal-title":"C R Biol"},{"issue":"1","key":"pone.0354469.ref045","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0020-1790(89)90015-2","article-title":"\u03b2-Glucosidase in four phytophagous Lepidoptera","volume":"19","author":"SJ Yu","year":"1989","journal-title":"Insect Biochemistry"},{"issue":"7","key":"pone.0354469.ref046","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/j.crvi.2009.02.009","article-title":"Enzymatic properties of alpha- and beta-glocusidases extracted from midgut and salivary glands of rice striped stem borer, Chilo suppressalis Walker (Lepidoptera: Pyralidae)","volume":"332","author":"A Zibaee","year":"2009","journal-title":"C R Biol"},{"key":"pone.0354469.ref047","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.pisc.2014.02.002","article-title":"Standardization in enzymology\u2014Data integration in the world\u05f3s enzyme information system BRENDA","volume":"1","author":"I Schomburg","year":"2014","journal-title":"Perspectives in Science"},{"issue":"10","key":"pone.0354469.ref048","doi-asserted-by":"crossref","first-page":"3223","DOI":"10.1007\/s10562-018-2504-3","article-title":"Functional Characterization of a New Cold-Adapted \u03b2-Galactosidase from an Arctic Fjord Sediment Bacteria Enterobacter ludwigii MCC 3423","volume":"148","author":"AP Alikunju","year":"2018","journal-title":"Catal Lett"},{"key":"pone.0354469.ref049","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.carbpol.2017.01.033","article-title":"Preparation and characterization of gellan gum microspheres containing a cold-adapted \u03b2-galactosidase from Rahnella sp. R3","volume":"162","author":"Y Fan","year":"2017","journal-title":"Carbohydr Polym"},{"key":"pone.0354469.ref050","first-page":"11842","article-title":"Extraction, purification and characterization of \u03b2-galactosidase from tomato (Lycopersicon esculentum) and its application in milk","volume":"25","author":"SA Hussien","year":"2021","journal-title":"Annals of Romanian Society for Cell Biology"},{"issue":"3","key":"pone.0354469.ref051","doi-asserted-by":"crossref","first-page":"1190","DOI":"10.1007\/s12010-020-03233-w","article-title":"Purification and Characterization of a Novel \u03b2-Galactosidase From the Thermoacidophile Alicyclobacillus vulcanalis","volume":"191","author":"J Murphy","year":"2020","journal-title":"Appl Biochem Biotechnol"},{"issue":"6","key":"pone.0354469.ref052","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1007\/s00792-019-01133-4","article-title":"Purification and characterization of a novel thermophilic \u03b2-galactosidase from Picrophilus torridus of potential industrial application","volume":"23","author":"J Murphy","year":"2019","journal-title":"Extremophiles"},{"key":"pone.0354469.ref053","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1016\/j.ijbiomac.2020.04.013","article-title":"Purification, characterization and specificity of a new GH family 35 galactosidase from Aspergillus awamori","volume":"156","author":"CH Vidya","year":"2020","journal-title":"Int J Biol Macromol"},{"issue":"7","key":"pone.0354469.ref054","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0302679","article-title":"Theory on the rate equations of Michaelis-Menten type enzyme kinetics with competitive inhibition","volume":"19","author":"R Murugan","year":"2024","journal-title":"PLoS One"},{"issue":"1","key":"pone.0354469.ref055","doi-asserted-by":"crossref","first-page":"2739","DOI":"10.1038\/s41467-025-57327-2","article-title":"High-order Michaelis-Menten equations allow inference of hidden kinetic parameters in enzyme catalysis","volume":"16","author":"D Singh","year":"2025","journal-title":"Nat Commun"},{"issue":"10","key":"pone.0354469.ref056","first-page":"5010","article-title":"Thermal stability and kinetic characterization of insect-derived glycosidases using the Arrhenius model","volume":"9","author":"KS Marius","year":"2025","journal-title":"Trop J Nat Prod Res"},{"key":"pone.0354469.ref057","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1080\/08948550302453","article-title":"A Century of Enzyme Kinetics: Reliability of the K M and v max Estimates","volume":"8","author":"PK Maini","year":"2003","journal-title":"Comments on Theoretical Biology"}],"container-title":["PLOS One"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0354469","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T17:41:40Z","timestamp":1784742100000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0354469"}},"subtitle":[],"editor":[{"given":"Rafael","family":"Vazquez-Duhalt","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2026,7,22]]},"references-count":57,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2026,7,22]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0354469","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,22]]}}}