Cross-linked alpha-galactosidase aggregates: optimization, characterization and application in the hydrolysis of raffinose-type oligosaccharides in soymilk

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dc.contributor.authorBayraktar, Hasan
dc.contributor.authorOnal, Secil
dc.date.accessioned2019-10-27T09:41:58Z
dc.date.available2019-10-27T09:41:58Z
dc.date.issued2019
dc.departmentEge Üniversitesien_US
dc.description.abstractBACKGROUND Cross-linked enzyme aggregates (CLEAs) of alpha-galactosidase, partially purified from maize (Zea mays) flour, were prepared. The impact of various parameters on enzyme activity was examined to optimize the immobilization procedure. Biochemical characterization of the free and immobilized enzyme was carried out. Stability (thermal, pH, storage and operational stability) and reusability tests were performed. The potential use of the free enzyme and the CLEAs in hydrolysis processes of raffinose-type oligosaccharides present in soymilk was investigated. RESULTS alpha-galactosidase CLEAs were prepared with 47% activity recovery under optimum conditions [1:5 (v/v) enzyme solution:saturated ammonium sulfate solution ratio; 7.5 mg protein and 0.1% (v/v) glutaraldehyde, 6 h, 4 degrees C, 150 rpm]. alpha-galactosidase CLEAs exhibited increased stability in comparison to the free enzyme. The CLEAs and the free enzyme showed a maximum activity at 40 degrees C and their optimal pH values were5.5 and 6.0, respectively. Kinetic constants (K-M, V-max and k(cat)) were calculated for the free enzyme and the CLEAs in the presence of p-nitrophenyl-alpha-d-galactopyranoside, stachyose, melibiose and raffinose. The effect of various chemicals and sugars on enzyme activity showed that both enzyme forms were significantly inhibited by HgCl2 and galactose. The CLEAs hydrolyzed 85% of raffinose and 96% of stachyose. CONCLUSION The alpha-galactosidase CLEAs, with their satisfactory enzymatic characteristics, have much potential for use in the food and feed industry. (c) 2019 Society of Chemical Industryen_US
dc.description.sponsorshipEge University Research FoundationEge University [2013 FEN 022]en_US
dc.description.sponsorshipThis work was funded by the Ege University Research Foundation (Project 2013 FEN 022).en_US
dc.identifier.doi10.1002/jsfa.9720en_US
dc.identifier.endpage4760en_US
dc.identifier.issn0022-5142
dc.identifier.issn1097-0010
dc.identifier.issue10en_US
dc.identifier.pmid30932192en_US
dc.identifier.startpage4748en_US
dc.identifier.urihttps://doi.org/10.1002/jsfa.9720
dc.identifier.urihttps://hdl.handle.net/11454/28696
dc.identifier.volume99en_US
dc.identifier.wosWOS:000471905200028en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.relation.ispartofJournal of the Science of Food and Agricultureen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectmaize (Zea mays)en_US
dc.subjectalpha-galactosidaseen_US
dc.subjectcross-linked enzyme aggregatesen_US
dc.subjectCLEAsen_US
dc.subjectsoymilken_US
dc.subjectraffinose-type oligosaccharidesen_US
dc.titleCross-linked alpha-galactosidase aggregates: optimization, characterization and application in the hydrolysis of raffinose-type oligosaccharides in soymilken_US
dc.typeArticleen_US

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