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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agroindústria de Alimentos. Para informações adicionais entre em contato com ctaa.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Agroenergia; Embrapa Agroindústria de Alimentos. |
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Data corrente: |
04/03/2022 |
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Data da última atualização: |
10/10/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
SANTOS, A. DA S.; PEREIRA, G. M.; ALMEIDA, A. M. M. DE; SANTOS, R. R. DOS; TERZI, S. da C.; PACHECO, T. F.; VERMELHO, A. B.; CABRAL, L. M. C.; COURI, S.; DAMASO, M. C. T. |
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Afiliação: |
ALEX DA SILVA SANTOS, Univesidade Federal Rural do Rio de Janeiro - UFRRJ; GABRIELA MOYSES PEREIRA, Universidade Federal do Rio de Janeiro - UFRJ; ANA MARIA MAZOTTO DE ALMEIDA, Universidade Federal do Rio de Janeiro - UFRJ; REGIANE RIBEIRO DOS SANTOS, Universidade Federal Rural do Rio de Janeiro - UFRRJ; SELMA DA COSTA TERZI, CTAA; THALYTA FRAGA PACHECO, Universidade Federal do Rio de Janeiro - UFRJ; ALANE BEATRIZ VERMELHO, Universidade Federal do Rio de Janeiro - UFRJ; LOURDES MARIA CORREA CABRAL, CTAA; SONIA COURI, CTAA; MONICA CARAMEZ TRICHES DAMASO, CNPAE. |
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Título: |
Production, concentration and partial characterization of an enzymatic extract produced by an Aspergillus niger mutant in solid state fermentation. |
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Ano de publicação: |
2022 |
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Fonte/Imprenta: |
Preparative Biochemistry & Biotechnology, 2022. |
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DOI: |
https://doi.org/10.1080/10826068.2022.2033989 |
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Idioma: |
Inglês |
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Notas: |
Early Access. |
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Conteúdo: |
An enzymatic extract from Aspergillus niger 3T5B8 was produced by Solid State Fermentation (SSF) in aerated columns, using wheat bran as substrate. A combination of extracts produced using three different process conditions varying temperature, pH and aeration formed the final extract (Mixture). The Mixture was concentrated by an ultrafiltration process that partially purified and provided an efficient recovery of the enzymatic activities of xylanase (88.89%), polygalacturonase (89.3%), beta-glucosidase (93.15%), protease (98.68%) and carboxymethylcellulase (CMCase) (98.93%). SDS-PAGE analysis showed 15 visible protein bands in the crude and concentrated Mixture with molecular weights ranging from 15.1 to 104.6 kDa. Thin layer chromatography confirmed the effective action of beta-glucosidase and xylanase hydrolysis activities over cellobiose and xylan, respectively. A central composite design (CCD) with two variables and four replicates at the center points was used to determine the optimal temperature and pH for CMCase and beta-glucosidase. The optimal temperature was 78.9 degrees C and pH 3.8 for CMCase and 52.8 degrees C and pH 4.8 for beta-glucosidase, respectively. |
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Palavras-Chave: |
Aspergillus niger 3T5B8; Cellulolytic enzymes; Enzyme concentration; Partial characterization. |
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Thesagro: |
Aspergillus Niger. |
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Thesaurus Nal: |
Enzymes; Solid state fermentation; Ultrafiltration. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02304naa a2200349 a 4500
001 2140582
005 2022-10-10
008 2022 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1080/10826068.2022.2033989$2DOI
100 1 $aSANTOS, A. DA S.
245 $aProduction, concentration and partial characterization of an enzymatic extract produced by an Aspergillus niger mutant in solid state fermentation.$h[electronic resource]
260 $c2022
500 $aEarly Access.
520 $aAn enzymatic extract from Aspergillus niger 3T5B8 was produced by Solid State Fermentation (SSF) in aerated columns, using wheat bran as substrate. A combination of extracts produced using three different process conditions varying temperature, pH and aeration formed the final extract (Mixture). The Mixture was concentrated by an ultrafiltration process that partially purified and provided an efficient recovery of the enzymatic activities of xylanase (88.89%), polygalacturonase (89.3%), beta-glucosidase (93.15%), protease (98.68%) and carboxymethylcellulase (CMCase) (98.93%). SDS-PAGE analysis showed 15 visible protein bands in the crude and concentrated Mixture with molecular weights ranging from 15.1 to 104.6 kDa. Thin layer chromatography confirmed the effective action of beta-glucosidase and xylanase hydrolysis activities over cellobiose and xylan, respectively. A central composite design (CCD) with two variables and four replicates at the center points was used to determine the optimal temperature and pH for CMCase and beta-glucosidase. The optimal temperature was 78.9 degrees C and pH 3.8 for CMCase and 52.8 degrees C and pH 4.8 for beta-glucosidase, respectively.
650 $aEnzymes
650 $aSolid state fermentation
650 $aUltrafiltration
650 $aAspergillus Niger
653 $aAspergillus niger 3T5B8
653 $aCellulolytic enzymes
653 $aEnzyme concentration
653 $aPartial characterization
700 1 $aPEREIRA, G. M.
700 1 $aALMEIDA, A. M. M. DE
700 1 $aSANTOS, R. R. DOS
700 1 $aTERZI, S. da C.
700 1 $aPACHECO, T. F.
700 1 $aVERMELHO, A. B.
700 1 $aCABRAL, L. M. C.
700 1 $aCOURI, S.
700 1 $aDAMASO, M. C. T.
773 $tPreparative Biochemistry & Biotechnology, 2022.
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