Immobilization of alpha acetolactate decarboxylase in hybrid gelatin/alginate support for application to reduce diacetyl off-flavor in beer

Detalhes bibliográficos
Autor(a) principal: Costa, Gustavo Pires
Data de Publicação: 2023
Outros Autores: Queiroz, Leonardo Braun Pinto de, Manfroi, Vitor, Rodrigues, Rafael Costa, Hertz, Plinho Francisco
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFRGS
Texto Completo: http://hdl.handle.net/10183/262336
Resumo: Beer production is the largest among alcoholic beverages. Its production process is complex and demands several steps. Lager beers commonly present an off-flavor of butter that is due to the presence of diacetyl, and to avoid such a problem, a long period of maturation (3–5 weeks) is required. Another way is the application of (α-acetolactate decarboxylase) ALDC to accelerate the process. The objectives of the present work were to develop a low-cost support using gelatin, a residue from capsules from the nutraceutical industry, to immobilize the ALDC enzyme. For this, the yield, efficiency and activity recovered, and the stability of free and immobilized enzymes at different temperatures and pH were evaluated. To evaluate the capacity of immobilized enzymes when applied directly to beer and their operational stability, three concentrations of glutaraldehyde (1%, 2.5% and 5%) were tested in distilled water as a cross-linking agent. The best results obtained were 95.6%, 27.0% and 23.6%, respectively, for yield, efficiency and activity recovery. Immobilization provided a high activity over a wide pH range. The immobilized enzyme showed greater stability at temperatures of 50 and 60 ◦C. The immobilized derivative showed adequate reuse capacity, and its dehydrated form had excellent activity after long periods of storage.
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spelling Costa, Gustavo PiresQueiroz, Leonardo Braun Pinto deManfroi, VitorRodrigues, Rafael CostaHertz, Plinho Francisco2023-07-19T03:38:48Z20232073-4344http://hdl.handle.net/10183/262336001169149Beer production is the largest among alcoholic beverages. Its production process is complex and demands several steps. Lager beers commonly present an off-flavor of butter that is due to the presence of diacetyl, and to avoid such a problem, a long period of maturation (3–5 weeks) is required. Another way is the application of (α-acetolactate decarboxylase) ALDC to accelerate the process. The objectives of the present work were to develop a low-cost support using gelatin, a residue from capsules from the nutraceutical industry, to immobilize the ALDC enzyme. For this, the yield, efficiency and activity recovered, and the stability of free and immobilized enzymes at different temperatures and pH were evaluated. To evaluate the capacity of immobilized enzymes when applied directly to beer and their operational stability, three concentrations of glutaraldehyde (1%, 2.5% and 5%) were tested in distilled water as a cross-linking agent. The best results obtained were 95.6%, 27.0% and 23.6%, respectively, for yield, efficiency and activity recovery. Immobilization provided a high activity over a wide pH range. The immobilized enzyme showed greater stability at temperatures of 50 and 60 ◦C. The immobilized derivative showed adequate reuse capacity, and its dehydrated form had excellent activity after long periods of storage.application/pdfengCatalysts. Basel. Vol. 13, no. 3 (Mar. 2023), 601, 13 p.AlginatoGelatinaImobilização enzimáticaEstabilidade térmicaALDCImmobilizationAlginate/alginateGelatin residueImmobilization of alpha acetolactate decarboxylase in hybrid gelatin/alginate support for application to reduce diacetyl off-flavor in beerEstrangeiroinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSTEXT001169149.pdf.txt001169149.pdf.txtExtracted Texttext/plain58706http://www.lume.ufrgs.br/bitstream/10183/262336/2/001169149.pdf.txtd0c9e99d10ca37ec7f7f80b96fd12ea1MD52ORIGINAL001169149.pdfTexto completo (inglês)application/pdf2522455http://www.lume.ufrgs.br/bitstream/10183/262336/1/001169149.pdf00d643724fe85976589b0e6203a041ebMD5110183/2623362024-04-07 06:25:48.917095oai:www.lume.ufrgs.br:10183/262336Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2024-04-07T09:25:48Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false
dc.title.pt_BR.fl_str_mv Immobilization of alpha acetolactate decarboxylase in hybrid gelatin/alginate support for application to reduce diacetyl off-flavor in beer
title Immobilization of alpha acetolactate decarboxylase in hybrid gelatin/alginate support for application to reduce diacetyl off-flavor in beer
spellingShingle Immobilization of alpha acetolactate decarboxylase in hybrid gelatin/alginate support for application to reduce diacetyl off-flavor in beer
Costa, Gustavo Pires
Alginato
Gelatina
Imobilização enzimática
Estabilidade térmica
ALDC
Immobilization
Alginate/alginate
Gelatin residue
title_short Immobilization of alpha acetolactate decarboxylase in hybrid gelatin/alginate support for application to reduce diacetyl off-flavor in beer
title_full Immobilization of alpha acetolactate decarboxylase in hybrid gelatin/alginate support for application to reduce diacetyl off-flavor in beer
title_fullStr Immobilization of alpha acetolactate decarboxylase in hybrid gelatin/alginate support for application to reduce diacetyl off-flavor in beer
title_full_unstemmed Immobilization of alpha acetolactate decarboxylase in hybrid gelatin/alginate support for application to reduce diacetyl off-flavor in beer
title_sort Immobilization of alpha acetolactate decarboxylase in hybrid gelatin/alginate support for application to reduce diacetyl off-flavor in beer
author Costa, Gustavo Pires
author_facet Costa, Gustavo Pires
Queiroz, Leonardo Braun Pinto de
Manfroi, Vitor
Rodrigues, Rafael Costa
Hertz, Plinho Francisco
author_role author
author2 Queiroz, Leonardo Braun Pinto de
Manfroi, Vitor
Rodrigues, Rafael Costa
Hertz, Plinho Francisco
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Costa, Gustavo Pires
Queiroz, Leonardo Braun Pinto de
Manfroi, Vitor
Rodrigues, Rafael Costa
Hertz, Plinho Francisco
dc.subject.por.fl_str_mv Alginato
Gelatina
Imobilização enzimática
Estabilidade térmica
topic Alginato
Gelatina
Imobilização enzimática
Estabilidade térmica
ALDC
Immobilization
Alginate/alginate
Gelatin residue
dc.subject.eng.fl_str_mv ALDC
Immobilization
Alginate/alginate
Gelatin residue
description Beer production is the largest among alcoholic beverages. Its production process is complex and demands several steps. Lager beers commonly present an off-flavor of butter that is due to the presence of diacetyl, and to avoid such a problem, a long period of maturation (3–5 weeks) is required. Another way is the application of (α-acetolactate decarboxylase) ALDC to accelerate the process. The objectives of the present work were to develop a low-cost support using gelatin, a residue from capsules from the nutraceutical industry, to immobilize the ALDC enzyme. For this, the yield, efficiency and activity recovered, and the stability of free and immobilized enzymes at different temperatures and pH were evaluated. To evaluate the capacity of immobilized enzymes when applied directly to beer and their operational stability, three concentrations of glutaraldehyde (1%, 2.5% and 5%) were tested in distilled water as a cross-linking agent. The best results obtained were 95.6%, 27.0% and 23.6%, respectively, for yield, efficiency and activity recovery. Immobilization provided a high activity over a wide pH range. The immobilized enzyme showed greater stability at temperatures of 50 and 60 ◦C. The immobilized derivative showed adequate reuse capacity, and its dehydrated form had excellent activity after long periods of storage.
publishDate 2023
dc.date.accessioned.fl_str_mv 2023-07-19T03:38:48Z
dc.date.issued.fl_str_mv 2023
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dc.identifier.issn.pt_BR.fl_str_mv 2073-4344
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dc.relation.ispartof.pt_BR.fl_str_mv Catalysts. Basel. Vol. 13, no. 3 (Mar. 2023), 601, 13 p.
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