Characterization and winemaking application of a novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235
- Autores
- Fratebianchi de la Parra, Dante; González, M.; Tenorio, C.; Cavalitto, Sebastián Fernando; Ruiz-Larrea, F.
- Año de publicación
- 2017
- Idioma
- español castellano
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- A novel pectin-degrading enzyme complex produced by Aspergillus sojae ATCC 20235 (PC-AS) using lowcost substrates was characterised in terms of its enzyme activities relevant in winemaking. This novel PC-AS was applied at the maceration/fermentation stage during the elaboration of 'Tempranillo' red wines to study its effect on colour development and the phenolic and amino acid wine composition. PC-AS polygalacturonase activity was the major enzyme activity detected and quantified under winemaking conditions (pH 3.5, 20 °C) and proved being stable and active in the presence of sulfur dioxide. Xylanase activity, albeit in lesser amounts, was also present in PC-AS, and neither pectinesterase, which produces methanol, nor β-glucosidase, which is detrimental to wine colour, were detected in PC-AS. This pectin-degrading complex promoted a faster colour extraction since maximum colour intensity of the enzyme treated wines was reached earlier compared to their controls. After 6 months of storage under winery conditions, wines elaborated with PC-AS presented higher concentrations of caffeic acid, coumaric acid and aspartic acid (p ˂ 0.05), suggesting an improved extraction of grape cell components. In conclusion, the application of PCAS yielded results that showed that it can be used in red winemaking to shorten the maceration time needed to reach high CI values and to improve the extraction of some phenolics and other compounds that enhance the quality of the final product.
Facultad de Ciencias Exactas
Centro de Investigación y Desarrollo en Fermentaciones Industriales - Materia
-
Química
Aspergillus sojae
red wine
pectinases
colour
phenolics - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/78632
Ver los metadatos del registro completo
id |
SEDICI_eb43c2149ffa529a3b59ea68b8b9b971 |
---|---|
oai_identifier_str |
oai:sedici.unlp.edu.ar:10915/78632 |
network_acronym_str |
SEDICI |
repository_id_str |
1329 |
network_name_str |
SEDICI (UNLP) |
spelling |
Characterization and winemaking application of a novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235Fratebianchi de la Parra, DanteGonzález, M.Tenorio, C.Cavalitto, Sebastián FernandoRuiz-Larrea, F.QuímicaAspergillus sojaered winepectinasescolourphenolicsA novel pectin-degrading enzyme complex produced by Aspergillus sojae ATCC 20235 (PC-AS) using lowcost substrates was characterised in terms of its enzyme activities relevant in winemaking. This novel PC-AS was applied at the maceration/fermentation stage during the elaboration of 'Tempranillo' red wines to study its effect on colour development and the phenolic and amino acid wine composition. PC-AS polygalacturonase activity was the major enzyme activity detected and quantified under winemaking conditions (pH 3.5, 20 °C) and proved being stable and active in the presence of sulfur dioxide. Xylanase activity, albeit in lesser amounts, was also present in PC-AS, and neither pectinesterase, which produces methanol, nor β-glucosidase, which is detrimental to wine colour, were detected in PC-AS. This pectin-degrading complex promoted a faster colour extraction since maximum colour intensity of the enzyme treated wines was reached earlier compared to their controls. After 6 months of storage under winery conditions, wines elaborated with PC-AS presented higher concentrations of caffeic acid, coumaric acid and aspartic acid (p ˂ 0.05), suggesting an improved extraction of grape cell components. In conclusion, the application of PCAS yielded results that showed that it can be used in red winemaking to shorten the maceration time needed to reach high CI values and to improve the extraction of some phenolics and other compounds that enhance the quality of the final product.Facultad de Ciencias ExactasCentro de Investigación y Desarrollo en Fermentaciones Industriales2017-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf85-93http://sedici.unlp.edu.ar/handle/10915/78632spainfo:eu-repo/semantics/altIdentifier/issn/2367-4156info:eu-repo/semantics/altIdentifier/doi/10.5073/vitis.2017.56.85-93info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-sa/4.0/Creative Commons Attribution-ShareAlike 4.0 International (CC BY-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:14:13Zoai:sedici.unlp.edu.ar:10915/78632Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:14:13.807SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Characterization and winemaking application of a novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 |
title |
Characterization and winemaking application of a novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 |
spellingShingle |
Characterization and winemaking application of a novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 Fratebianchi de la Parra, Dante Química Aspergillus sojae red wine pectinases colour phenolics |
title_short |
Characterization and winemaking application of a novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 |
title_full |
Characterization and winemaking application of a novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 |
title_fullStr |
Characterization and winemaking application of a novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 |
title_full_unstemmed |
Characterization and winemaking application of a novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 |
title_sort |
Characterization and winemaking application of a novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 |
dc.creator.none.fl_str_mv |
Fratebianchi de la Parra, Dante González, M. Tenorio, C. Cavalitto, Sebastián Fernando Ruiz-Larrea, F. |
author |
Fratebianchi de la Parra, Dante |
author_facet |
Fratebianchi de la Parra, Dante González, M. Tenorio, C. Cavalitto, Sebastián Fernando Ruiz-Larrea, F. |
author_role |
author |
author2 |
González, M. Tenorio, C. Cavalitto, Sebastián Fernando Ruiz-Larrea, F. |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Química Aspergillus sojae red wine pectinases colour phenolics |
topic |
Química Aspergillus sojae red wine pectinases colour phenolics |
dc.description.none.fl_txt_mv |
A novel pectin-degrading enzyme complex produced by Aspergillus sojae ATCC 20235 (PC-AS) using lowcost substrates was characterised in terms of its enzyme activities relevant in winemaking. This novel PC-AS was applied at the maceration/fermentation stage during the elaboration of 'Tempranillo' red wines to study its effect on colour development and the phenolic and amino acid wine composition. PC-AS polygalacturonase activity was the major enzyme activity detected and quantified under winemaking conditions (pH 3.5, 20 °C) and proved being stable and active in the presence of sulfur dioxide. Xylanase activity, albeit in lesser amounts, was also present in PC-AS, and neither pectinesterase, which produces methanol, nor β-glucosidase, which is detrimental to wine colour, were detected in PC-AS. This pectin-degrading complex promoted a faster colour extraction since maximum colour intensity of the enzyme treated wines was reached earlier compared to their controls. After 6 months of storage under winery conditions, wines elaborated with PC-AS presented higher concentrations of caffeic acid, coumaric acid and aspartic acid (p ˂ 0.05), suggesting an improved extraction of grape cell components. In conclusion, the application of PCAS yielded results that showed that it can be used in red winemaking to shorten the maceration time needed to reach high CI values and to improve the extraction of some phenolics and other compounds that enhance the quality of the final product. Facultad de Ciencias Exactas Centro de Investigación y Desarrollo en Fermentaciones Industriales |
description |
A novel pectin-degrading enzyme complex produced by Aspergillus sojae ATCC 20235 (PC-AS) using lowcost substrates was characterised in terms of its enzyme activities relevant in winemaking. This novel PC-AS was applied at the maceration/fermentation stage during the elaboration of 'Tempranillo' red wines to study its effect on colour development and the phenolic and amino acid wine composition. PC-AS polygalacturonase activity was the major enzyme activity detected and quantified under winemaking conditions (pH 3.5, 20 °C) and proved being stable and active in the presence of sulfur dioxide. Xylanase activity, albeit in lesser amounts, was also present in PC-AS, and neither pectinesterase, which produces methanol, nor β-glucosidase, which is detrimental to wine colour, were detected in PC-AS. This pectin-degrading complex promoted a faster colour extraction since maximum colour intensity of the enzyme treated wines was reached earlier compared to their controls. After 6 months of storage under winery conditions, wines elaborated with PC-AS presented higher concentrations of caffeic acid, coumaric acid and aspartic acid (p ˂ 0.05), suggesting an improved extraction of grape cell components. In conclusion, the application of PCAS yielded results that showed that it can be used in red winemaking to shorten the maceration time needed to reach high CI values and to improve the extraction of some phenolics and other compounds that enhance the quality of the final product. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-04 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/78632 |
url |
http://sedici.unlp.edu.ar/handle/10915/78632 |
dc.language.none.fl_str_mv |
spa |
language |
spa |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/2367-4156 info:eu-repo/semantics/altIdentifier/doi/10.5073/vitis.2017.56.85-93 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-sa/4.0/ Creative Commons Attribution-ShareAlike 4.0 International (CC BY-SA 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-sa/4.0/ Creative Commons Attribution-ShareAlike 4.0 International (CC BY-SA 4.0) |
dc.format.none.fl_str_mv |
application/pdf 85-93 |
dc.source.none.fl_str_mv |
reponame:SEDICI (UNLP) instname:Universidad Nacional de La Plata instacron:UNLP |
reponame_str |
SEDICI (UNLP) |
collection |
SEDICI (UNLP) |
instname_str |
Universidad Nacional de La Plata |
instacron_str |
UNLP |
institution |
UNLP |
repository.name.fl_str_mv |
SEDICI (UNLP) - Universidad Nacional de La Plata |
repository.mail.fl_str_mv |
alira@sedici.unlp.edu.ar |
_version_ |
1844616013541277696 |
score |
13.070432 |