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- Title
Enzymatic treatment of soy protein isolates: effects on the potential allergenicity, technofunctionality, and sensory properties.
- Authors
Meinlschmidt, Pia; Sussmann, Daniela; Schweiggert‐Weisz, Ute; Eisner, Peter
- Abstract
Soybean allergy is of great concern and continues to challenge both consumer and food industry. The present study investigates the enzyme-assisted reduction in major soybean allergens in soy protein isolate using different food-grade proteases, while maintaining or improving the sensory attributes and technofunctional properties. SDS- PAGE analyses showed that hydrolysis with Alcalase, Pepsin, and Papain was most effective in the degradation of the major soybean allergens with proteolytic activities of 100%, 100%, and 95.9%, respectively. In the course of hydrolysis, the degree of hydrolysis increased, and Alcalase showed the highest degree of hydrolysis (13%) among the proteases tested. DSC analysis confirmed the degradation of major soybean allergens. The sensory experiments conducted by a panel of 10 panelists considered the overall improved sensory properties as well as the bitterness of the individual hydrolysates. In particular, Flavourzyme and Papain were attractive due to a less pronounced bitter taste and improved sensory profile (smell, taste, mouthfeeling). Technofunctional properties showed a good solubility at pH 7.0 and 4.0, emulsifying capacity up to 760 mL g−1 (Flavourzyme) as well as improved oil-binding capacities, while the water-binding properties were generally decreased. Increased foaming activity for all proteases up to 3582% (Pepsin) was observed, whereas lower foaming stability and density were found. The hydrolysates could potentially be used as hypoallergenic ingredients in a variety of food products due to their improved technofunctional properties and a pleasant taste.
- Subjects
SOY proteins; FOOD allergy; HYDROLYSIS; PAPAIN; PEPSIN; SENSORY evaluation
- Publication
Food Science & Nutrition, 2016, Vol 4, Issue 1, p11
- ISSN
2048-7177
- Publication type
Article
- DOI
10.1002/fsn3.253