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Characterization of recombinant human lysosomal beta-hexosaminidases produced in the methylotrophic yeast Pichia pastoris

dc.contributorAdministrative Department of Science, Technology and Innovation COLCIENCIAS and Pontificia Universidad Javeriana
dc.creatorEspejo Mojica, Angela Johana; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana. Bogotá, Colombia
dc.creatorMosquera, Angela Rocío; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana. Bogotá, Colombia
dc.creatorRodríguez-López, Edwin Alexander; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana. Bogotá, Colombia Chemistry Department, School of Science, Pontificia Universidad Javeriana, Bogotá, Colombia
dc.creatorDíaz, Dennis Johana; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana. Bogotá, Colombia
dc.creatorBetrán, Laura Milena; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana. Bogotá, Colombia
dc.creatorHernández, Francy Liliana; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana. Bogotá, Colombia
dc.creatorAlméciga Díaz, Carlos Javier; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana. Bogotá, Colombia
dc.creatorBarrera, Luis Alejandro; Institute for the Study of Inborn Errors of Metabolism, School of Sciences, Pontificia Universidad Javeriana. Bogotá, Colombia Clínica de Errores Innatos del Metabolismo. Hospital Universitario San Ignacio. Bogotá, Colombia.
dc.date2018-02-24T15:59:28Z
dc.date2020-04-15T18:10:16Z
dc.date2018-02-24T15:59:28Z
dc.date2020-04-15T18:10:16Z
dc.date2016-09-29
dc.date.accessioned2025-10-30T13:19:23Z
dc.date.available2025-10-30T13:19:23Z
dc.identifierhttp://revistas.javeriana.edu.co/index.php/scientarium/article/view/15736
dc.identifier10.11144/Javeriana.SC21-3.corh
dc.identifier2027-1352
dc.identifier0122-7483
dc.identifierhttp://hdl.handle.net/10554/31211
dc.identifier.urihttp://test.repositoriodigital.com:8080/handle/123456789/179294
dc.descriptionβ-hexosaminidases (Hex) are dimeric enzymes involved in the lysosomal degradation of glycolipids and glycans. They are formed by α- and/or β-subunits encoded by HEXA and HEXB genes, respectively. Mutations in these genes lead to Tay Sachs or Sandhoff diseases, which are neurodegenerative disorders caused by the accumulation of non-degraded glycolipids. Although tissue-derived Hex have been widely characterized, limited information is available for recombinant β-hexosaminidases. In this study, human lysosomal recombinant Hex (rhHex-A, rhHex-B, and rhHex-S) were produced in the methylotrophic yeast Pichia pastoris GS115. The highest specific enzyme activities were 13,124 for rhHexA; 12,779 for rhHex-B; and 14.606 U.mg-1 for rhHex-S. These results were 25- to 50-fold higher than those obtained from normal human leukocytes. Proteins were purified and characterized at different pH and temperature conditions. All proteins were stable at acidic pH, and at4 °C and 37 °C. At 45 °C rhHex-S was completely inactivated, while rhHex-A and rhHex-B showed high stability. This study demonstrates P. pastoris GS115 potential for polymeric lysosomal enzyme production, and describes the characterization of recombinant β-hexosaminidases produced within the same host.
dc.formatPDF
dc.formatapplication/pdf
dc.languageeng
dc.publisherPontificia Universidad Javeriana
dc.relationhttp://revistas.javeriana.edu.co/index.php/scientarium/article/view/15736/13900
dc.relationhttp://revistas.javeriana.edu.co/index.php/scientarium/article/downloadSuppFile/15736/6984
dc.relationhttp://revistas.javeriana.edu.co/index.php/scientarium/article/downloadSuppFile/15736/6985
dc.relationhttp://revistas.javeriana.edu.co/index.php/scientarium/article/downloadSuppFile/15736/6987
dc.relationhttp://revistas.javeriana.edu.co/index.php/scientarium/article/downloadSuppFile/15736/6988
dc.relationhttp://revistas.javeriana.edu.co/index.php/scientarium/article/downloadSuppFile/15736/6989
dc.relationhttp://revistas.javeriana.edu.co/index.php/scientarium/article/downloadSuppFile/15736/6990
dc.relationhttp://revistas.javeriana.edu.co/index.php/scientarium/article/downloadSuppFile/15736/6991
dc.relationhttp://revistas.javeriana.edu.co/index.php/scientarium/article/downloadSuppFile/15736/6992
dc.relationhttp://revistas.javeriana.edu.co/index.php/scientarium/article/downloadSuppFile/15736/6993
dc.relationUniversitas Scientiarum; Vol 21, No 3 (2016); 195-217
dc.relationUniversitas Scientiarum; Vol 21, No 3 (2016); 195-217
dc.relationUniversitas Scientiarum; Vol 21, No 3 (2016); 195-217
dc.rightsCopyright (c) 2016 Universitas Scientiarum
dc.rightsAtribución-NoComercial-SinDerivadas 4.0 Internacional
dc.rightshttp://creativecommons.org/licenses/by-nc/4.0
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightshttp://purl.org/coar/access_right/c_abf2
dc.subjectBiotechnology
dc.subjectβ-N-acetylhexosaminidases; characterization; Pichia pastoris; recombinant hexosaminidases; Sandhoff disease; Tay Sachs disease.
dc.titleCharacterization of recombinant human lysosomal beta-hexosaminidases produced in the methylotrophic yeast Pichia pastoris
dc.typehttp://purl.org/coar/version/c_970fb48d4fbd8a85
dc.typeArtículo de revista
dc.typehttp://purl.org/coar/resource_type/c_6501
dc.typeinfo:eu-repo/semantics/article
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