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dc.date.accessioned | 2022-11-23T17:22:08Z | |
dc.date.available | 2022-11-23T17:22:08Z | |
dc.date.issued | 2016-05 | |
dc.identifier.uri | http://sedici.unlp.edu.ar/handle/10915/146292 | |
dc.description.abstract | The latex from the patagonic plant Philibertia gilliesii Hook. et Arn. (Apocynaceae) is a milky-white suspension containing a proteolytic system constituted by several cysteine endopeptidases. A proteolytic preparation (philibertain g) from the latex of P. gilliesii fruits was obtained and characterized to evaluate its potential use in bioprocesses. Philibertain g contained 1.2 g/L protein and a specific (caseinolytic) activity of 7.0 Ucas/mg protein. It reached 80 % of its maximum caseinolytic activity in the pH 7–10 range, retained 80 % of the original activity after 2 h of incubation at temperatures ranging from 25 to 45 °C and could be fully inactivated after 5 min at 75 °C. Philibertain g retained 60 % of the initial activity even at 1 M NaCl and was able to hydrolyze proteins from stickwater one, of the main waste effluents generated during fishmeal production. Furthermore, as a contribution to the knowledge of the proteolytic system of P. gilliesii, we are reporting the purification of a new peptidase, named philibertain g II (pI 9.4, molecular mass 23,977 Da, N-terminus LPESVDWREKGVVFPXRNQ) isolated from philibertain g through a purification scheme including acetone fractionation, cation exchange, molecular exclusion chromatography, and ultrafiltration. | en |
dc.format.extent | 332-346 | es |
dc.language | en | es |
dc.subject | Apocynaceae | es |
dc.subject | Chromatography | es |
dc.subject | Cysteine peptidase | es |
dc.subject | Fish protein hydrolysates | es |
dc.subject | Stickwater | es |
dc.title | The Proteolytic Activity of Philibertia gilliesii Latex | en |
dc.type | Articulo | es |
sedici.identifier.other | doi:10.1007/s12010-016-1997-8 | es |
sedici.identifier.other | pmid:26852027 | es |
sedici.identifier.issn | 1559-0291 | es |
sedici.identifier.issn | 0273-2289 | es |
sedici.title.subtitle | Purification of Philibertain g II | en |
sedici.creator.person | Sequeiros, Cynthia | es |
sedici.creator.person | Torres, María José | es |
sedici.creator.person | Nievas, Marina Lucrecia | es |
sedici.creator.person | Caffini, Néstor Oscar | es |
sedici.creator.person | Natalucci, Claudia Luisa | es |
sedici.creator.person | López, Laura María Isabel | es |
sedici.creator.person | Trejo, Sebastián Alejandro | es |
sedici.subject.materias | Ciencias Exactas | es |
sedici.subject.materias | Biología | es |
sedici.description.fulltext | true | es |
mods.originInfo.place | Centro de Investigación de Proteínas Vegetales | es |
sedici.subtype | Articulo | es |
sedici.rights.license | Creative Commons Attribution 4.0 International (CC BY 4.0) | |
sedici.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
sedici.description.peerReview | peer-review | es |
sedici.relation.journalTitle | Applied Biochemistry and Biotechnology | es |
sedici.relation.journalVolumeAndIssue | vol. 179, no. 2 | es |