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dc.contributor.author
Pacheco, Consuelo
dc.contributor.author
Crapiste, Guillermo Hector
dc.contributor.author
Carrin, Maria Elena
dc.date.available
2017-03-02T15:16:37Z
dc.date.issued
2015-09
dc.identifier.citation
Pacheco, Consuelo; Crapiste, Guillermo Hector; Carrin, Maria Elena; Study of acyl migration during enzymatic interesterification of liquid and fully hydrogenated soybean oil; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 122; 9-2015; 117-124
dc.identifier.issn
1381-1177
dc.identifier.uri
http://hdl.handle.net/11336/13464
dc.description.abstract
Lipase-catalyzed interesterification has emerged as an attractive process to obtain plastic fats because of its numerous advantages compared to the chemical reaction. The use of sn-1,3 specific lipases adds an even more interesting feature to this process, which is related to the possibility of maintaining the sn-2 fatty acid composition of natural substrates unaltered. The pursuit of this characteristic in interesterified products by sn-1,3 specific lipases could be threatened by a chemical reaction, the acyl migration whithin mono- and diacylglycerols. The aim of this study was to evaluate the occurrence of this undesired reaction in a soybean oil:fully hydrogenated soybean oil enzymatic interesterified blend. Once acyl migration was confirmed to occur, the influence of different reaction parameters -namely enzyme type and concentration, substrate ratio, and addition of hexane and temperature effect- was studied. Lipozyme TL IM demonstrated an enhancer acyl migration effect compared to Lipozyme RM IM, effect that was hypothesized to be correlated with the immobilization support material of the former (silica gel). Acyl migration was also promoted by the increase of biocatalyst concentration in reaction media. On the contrary, the presence of hexane, together with a decrease in temperature reaction, reduced its occurrence. A temperature effect analysis performed in solvent reaction media demonstrated its promoter effect on acyl migration.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Lipase-Catalyzed Interesterification
dc.subject
Acyl Migration
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Diacylglycerols
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Soybean Oil
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Fully Hydrogenated Soybean Oil
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Structured Lipids
dc.subject.classification
Otras Ingeniería Química
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Ingeniería Química
dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
dc.title
Study of acyl migration during enzymatic interesterification of liquid and fully hydrogenated soybean oil
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-03-01T17:49:03Z
dc.journal.volume
122
dc.journal.pagination
117-124
dc.journal.pais
Países Bajos
dc.journal.ciudad
Ámsterdam
dc.description.fil
Fil: Pacheco, Consuelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina. Universidad Nacional del Sur; Argentina
dc.description.fil
Fil: Crapiste, Guillermo Hector. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina. Universidad Nacional del Sur; Argentina
dc.description.fil
Fil: Carrin, Maria Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina. Universidad Nacional del Sur; Argentina
dc.journal.title
Journal of Molecular Catalysis B: Enzymatic
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1381117715300618
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.molcatb.2015.08.023


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