Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/46836

Titleß-galactosidase from Aspergillus lacticoffeatus: A promising biocatalyst for the synthesis of novel prebiotics
Author(s)Cardoso, B.
Silvério, Sara C.
Abrunhosa, Luís
Teixeira, J. A.
Rodrigues, L. R.
Keywordsß-galactosidase
Aspergillus lacticoffeatus
Industrial by-products
Prebiotics
Whole cells
Ochratoxin A
β-galactosidase
Issue date18-Sep-2017
PublisherElsevier
JournalInternational Journal of Food Microbiology
CitationCardoso, B.; Silvério, Sara C.; Abrunhosa, Luís; Teixeira, José A.; Rodrigues, Lígia R., beta-galactosidase from Aspergillus lacticoffeatus: A promising biocatalyst for the synthesis of novel prebiotics. International Journal of Food Microbiology, 257, 67-74, 2017
Abstract(s)ß-galactosidase (EC 3.2.1.23) are interesting enzymes able to catalyze lactose hydrolysis and transfer reactions to produce lactose-based prebiotics with potential application in the pharmaceutical and food industry. In this work, Aspergillus lacticoffeatus is described, for the first time, as an effective -galactosidase producer. The extracellular enzyme production was evaluated in synthetic and alternative media containing cheese whey and corn steep liquor. Although -galactosidase production occurred in all media (expect for the one composed solely by cheese whey), the highest enzymatic activity values (460 U/mL) were obtained for the synthetic medium. Ochratoxin A production in synthetic medium was also evaluated and 9 days of fermentation was identified as a suitable fermentation time to obtain a crude extract enzyme with mycotoxin concentration below the legal comparable value established for wine and grape juices (2 ng/mL). The optimal pH and temperature for the crude extract enzyme was found in the range of 3.54.5 and 5060 °C, respectively. The -galactosidase activity was reduced in the presence of Ba2 +, Fe2 +, Li+, K+ and galactose, while additives (except for ascorbic acid) and detergents exhibited a positive effect on enzymatic activity. This enzyme was able to catalyze the synthesis of prebiotics, namely lactulose (2.5 g/L) and a galacto-oligosaccharide (trisaccharide, 6.3 g/L), either when whole cells or crude enzyme was used as biocatalyst. The lactulose production using fungal whole cells is herein reported for the first time. Additionally, A. lacticoffeatus was also found to produce an enzyme with fructosyltransferase activity and other prebiotics, namely fructo-oligosaccharide 1-kestose (2.4 g/L).
TypeArticle
URIhttp://hdl.handle.net/1822/46836
DOI10.1016/j.ijfoodmicro.2017.06.013
ISSN0168-1605
e-ISSN0168-1605
Publisher versionhttp://www.journals.elsevier.com/international-journal-of-food-microbiology/
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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