{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,10]],"date-time":"2026-03-10T05:01:54Z","timestamp":1773118914435,"version":"3.50.1"},"reference-count":104,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2021,6,4]],"date-time":"2021-06-04T00:00:00Z","timestamp":1622764800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2021,6,4]],"date-time":"2021-06-04T00:00:00Z","timestamp":1622764800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Biotechnol"],"published-print":{"date-parts":[[2021,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec>\n                <jats:title>Background<\/jats:title>\n                <jats:p>Laccases (EC 1.10.3.2) are multi-copper oxidoreductases with great biotechnological importance due to their high oxidative potential and utility for removing synthetic dyes, oxidizing phenolic compounds, and degrading pesticides, among others.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Methods<\/jats:title>\n                <jats:p>A real-time stability study (RTS) was conducted for a year, by using enzyme concentrates from 3 batches (L1, L3, and L4). For which, five temperatures 243.15, 277.15, 298.15, 303.15, 308.15, and 313.15\u2009K were assayed. Using RTS data and the Arrhenius equation, we calculated the rPOXA 1B accelerated stability (AS). Molecular dynamics (MD) computational study results were very close to those obtained experimentally at four different temperatures 241, 278, 298, and 314\u2009K.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Results<\/jats:title>\n                <jats:p>In the RTS, 101.16, 115.81, 75.23, 46.09, 5.81, and 4.83% of the relative enzyme activity were recovered, at respective assayed temperatures. AS study, showed that rPOXA 1B is stable at 240.98\u2009\u00b1\u20095.38, 277.40\u2009\u00b1\u20091.32 or 297.53\u2009\u00b1\u20093.88\u2009K; with t<jats:sub>1\/2<\/jats:sub> values of 230.8, 46.2, and 12.6\u2009months, respectively. Kinetic and thermodynamic parameters supported the high stability of rPOXA 1B, with an <jats:italic>E<\/jats:italic><jats:sub><jats:italic>d<\/jats:italic><\/jats:sub> value of 41.40 KJ mol<jats:sup>\u2212\u20091<\/jats:sup>, a low variation of <jats:italic>K<\/jats:italic><jats:sub><jats:italic>M<\/jats:italic><\/jats:sub> and <jats:italic>V<\/jats:italic><jats:sub><jats:italic>max<\/jats:italic><\/jats:sub>, at 240.98\u2009\u00b1\u20095.38, and 297.53\u2009\u00b1\u20093.88\u2009K, and \u2206G values showing deactivation reaction does not occur. The MD indicates that fluctuations in loop, coils or loops with hydrophilic or intermediate polarity amino acids as well as in some residues of POXA 1B 3D structure, increases with temperature; changing from three fluctuating residues at 278\u2009K to six residues at 298\u2009K, and nine residues at 314\u2009K.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Conclusions<\/jats:title>\n                <jats:p>Laccase rPOXA 1B demonstrated experimentally and computationally to be a stable enzyme, with t<jats:sub>1\/2<\/jats:sub> of 230.8, 46.2 or 12.6\u2009months, if it is preserved impure without preservatives at temperatures of 240.98\u2009\u00b1\u20095.38, 277.40\u2009\u00b1\u20091.32 or 297.53\u2009\u00b1\u20093.88\u2009K respectively; this study could be of great utility for large scale producers.<\/jats:p>\n              <\/jats:sec>","DOI":"10.1186\/s12896-021-00698-3","type":"journal-article","created":{"date-parts":[[2021,6,4]],"date-time":"2021-06-04T20:02:46Z","timestamp":1622836966000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Recombinant laccase rPOXA 1B real-time, accelerated and molecular dynamics stability study"],"prefix":"10.1186","volume":"21","author":[{"given":"Leidy D.","family":"Ardila-Leal","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pedro A.","family":"Monterey-Guti\u00e9rrez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8841-2357","authenticated-orcid":false,"given":"Ra\u00fal A.","family":"Poutou-Pi\u00f1ales","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9875-2221","authenticated-orcid":false,"given":"Balkys E.","family":"Quevedo-Hidalgo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9968-362X","authenticated-orcid":false,"given":"Johan F.","family":"Galindo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Aura M.","family":"Pedroza-Rodr\u00edguez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2021,6,4]]},"reference":[{"issue":"3\u20134","key":"698_CR1","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1016\/j.fbr.2013.07.001","volume":"27","author":"CM Rivera-Hoyos","year":"2013","unstructured":"Rivera-Hoyos CM, Morales-\u00c1lvarez ED, Poutou-Pi\u00f1ales RA, Pedroza-Rodr\u00edguez AM, Rodr\u00edguez-V\u00e1zquez R, Delgado-Boada JM. 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