scispace - formally typeset
U

Ute Schweiggert-Weisz

Researcher at Fraunhofer Society

Publications -  52
Citations -  2023

Ute Schweiggert-Weisz is an academic researcher from Fraunhofer Society. The author has contributed to research in topics: Lupinus angustifolius & Chemistry. The author has an hindex of 19, co-authored 45 publications receiving 1205 citations.

Papers
More filters
Journal ArticleDOI

High moisture extrusion cooking of pea protein isolates: Raw material characteristics, extruder responses, and texture properties

TL;DR: In this paper, three commercial pea protein isolates were compared in order to investigate which protein properties affect extruder responses and product texture properties, and the comparison revealed that although their basic chemical compositions were similar their functional properties affected the viscosity of the protein mass during the initial heating phase of the extrusion process.
Journal ArticleDOI

Polyphenols as active ingredients for cosmetic products.

TL;DR: The effects of polyphenols in the context of anti‐ageing activity are summarized and some physicochemical aspects, namely the possible interactions with emulsifiers and the influence of the cosmetic formulation on the skin delivery, were reported.
Journal ArticleDOI

Inhibitory effects of polyphenols from grape pomace extract on collagenase and elastase activity.

TL;DR: In this article, extracts of pomace from Riesling grapes were analyzed for their inhibitory properties on collagenase as well as elastase, and the most pronounced impact was found for the hydrophilic low molecular weight polyphenols containing the free phenolic acids.
Journal ArticleDOI

Effect of high moisture extrusion cooking on protein–protein interactions of pea (Pisum sativum L.) protein isolates

TL;DR: In this article, protein alterations in fibrous meat substitutes produced by high moisture extrusion cooking of pea protein isolates were investigated and the structural integrity of extrudates could be attributed mainly to covalent disulphide bonding and, to a smaller extent, to non-covalent interactions.
Journal ArticleDOI

Enzymatic treatment of soy protein isolates: effects on the potential allergenicity, technofunctionality, and sensory properties

TL;DR: 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.