A novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 mutants.
J Sci Food Agric
; 95(7): 1554-61, 2015 May.
Article
em En
| MEDLINE
| ID: mdl-25103563
BACKGROUND: In the food industry, the use of pectinase preparations with high pectin esterase (PE) activity leads to the release of methanol, which is strictly regulated in food products. Herein, a pectin-degrading enzyme (PDE) complex exhibiting low PE activity of three Aspergillus sojae ATCC 20235 mutants (M3, DH56 and Guserbiot 2.230) was investigated. Production of exo-/endo-polygalacturonase (PG), exo-polymethylgalacturonase (PMG) and pectin lyase (PL) by mutant M3 and A. sojae using two different carbon sources was evaluated in solid-state fermentation. Finally, experimental preparations obtained from the mutants and commercial pectinases standardized to the same potency were screened for PDEs. RESULTS: Mutant M3 grown on sugar beet was found to be the best producer of exo-PG, endo-PG, exo-PMG and PL, with maximum yields of 1111, 449, 130 and 123 U g(-1), respectively. All experimental preparations exhibited low PE activity, at least 21.5 times less than commercial pectinases, and higher endo-PG (40 U mL(-1)). CONCLUSION: Mutant M3 was the best PDE producer using sugar beet. Mutant strains presented a PDE complex featuring high endo-PG and very low PE activities. This novel complex with low de-esterifying activity can be exploited in the food industry to degrade pectin without releasing methanol.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Poligalacturonase
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Aspergillus niger
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Pectinas
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Beta vulgaris
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Fermentação
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Complexos Multienzimáticos
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Mutação
Limite:
Humans
Idioma:
En
Revista:
J Sci Food Agric
Ano de publicação:
2015
Tipo de documento:
Article
País de afiliação:
México
País de publicação:
Reino Unido