Whey protein isolate hydrolysates obtained with free and immobilized Alcalase: Characterization and detection of residual allergens
Protein antigenicity can be reduced by enzymatic hydrolysis, which can be performed either by free or immobilized enzyme. The immobilized enzyme is removed from the reaction medium and reused, while the free enzyme must be inactivated to stop the reaction, generally by heating. Here we have shown th...
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Published in | Food research international Vol. 83; pp. 112 - 120 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier Ltd
01.05.2016
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Subjects | |
Online Access | Get full text |
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Summary: | Protein antigenicity can be reduced by enzymatic hydrolysis, which can be performed either by free or immobilized enzyme. The immobilized enzyme is removed from the reaction medium and reused, while the free enzyme must be inactivated to stop the reaction, generally by heating. Here we have shown that hydrolysates produced with free or immobilized Alcalase on glyoxyl-agarose bead presented different physicochemical properties (hydrophilicity profile, molecular mass distribution, surface hydrophobicity) and different levels of residual milk allergens (α-lactalbumin and β-lactoglobulin). Although, under the studied conditions, the hydrolysis with immobilized enzyme did not reduce the residual allergen levels as efficiently as the free enzyme, the results suggest potential applications of immobilized Alcalase for production of hypoallergenic hydrolysates.
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•At same conditions free or immobilized Alcalase produced different hydrolysates.•Hydrolysates with Immobilized Alcalase (ImA) showed lower degree of hydrolysis (DH).•Hydrolysates with Free Alcalase (FA) showed lower surface hydrophobicity (S0).•Only at pH8.0/ 65°C ImA and FA produced similar hydrolysates.•Hydrolysates with higher DH and lower S0 presented lower residual α-La and β-Lg levels. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0963-9969 1873-7145 |
DOI: | 10.1016/j.foodres.2016.02.015 |