TY - JOUR
T1 - Oat protein as plant-derived gelling agent
T2 - Properties and potential of modification
AU - Brückner-Gühmann, Monika
AU - Kratzsch, Annekatrin
AU - Sözer, Nesli
AU - Drusch, Stephan
N1 - Funding Information:
The project is part of the ERA-NET SUSFOOD “OATPRO, Engineering of oat proteins: Consumer driven sustainable food development process”. The authors thank the Federal Ministry of Education and Research, Germany (BMBF) Projektträger Jülich for the financial support (project no. 031A661).
PY - 2021/12
Y1 - 2021/12
N2 - The need for finding sustainable alternatives to animal originated proteins accelerates the development of plant-based innovations. Oat proteins are potential candidates as performance ingredient for tailoring taste and texture. Therefore, the ability of an oat protein isolate (OPI) and two oat protein hydrolysates to form heat-induced gels was analyzed at two pH conditions (4.5 and 8) as well as at two different temperatures (90 and 120 °C). The gelling properties were influenced by enzymatic hydrolysis with trypsin (OPT) and Alcalase® (OPA) to a degree of hydrolysis (DH) of 2%. Enzymatic modification altered the molecular weight distribution as well as the aggregation behavior of the oat protein which in turn affected the structural properties as well as the lightness of the gels. In detail, large aggregates led to an increased gel lightness. Alkaline conditions favored the browning of the gels. However, an increased protein aggregation in OPA-based gels improved the lightness under these conditions. This increased general understanding of the relationship between the overall functional properties of oat protein and its enzymatic modification will support the definition of targeted process windows for specific food applications. Therefore, enzymatic modification is a valuable tool to design plant protein ingredients with tailored functional properties.
AB - The need for finding sustainable alternatives to animal originated proteins accelerates the development of plant-based innovations. Oat proteins are potential candidates as performance ingredient for tailoring taste and texture. Therefore, the ability of an oat protein isolate (OPI) and two oat protein hydrolysates to form heat-induced gels was analyzed at two pH conditions (4.5 and 8) as well as at two different temperatures (90 and 120 °C). The gelling properties were influenced by enzymatic hydrolysis with trypsin (OPT) and Alcalase® (OPA) to a degree of hydrolysis (DH) of 2%. Enzymatic modification altered the molecular weight distribution as well as the aggregation behavior of the oat protein which in turn affected the structural properties as well as the lightness of the gels. In detail, large aggregates led to an increased gel lightness. Alkaline conditions favored the browning of the gels. However, an increased protein aggregation in OPA-based gels improved the lightness under these conditions. This increased general understanding of the relationship between the overall functional properties of oat protein and its enzymatic modification will support the definition of targeted process windows for specific food applications. Therefore, enzymatic modification is a valuable tool to design plant protein ingredients with tailored functional properties.
KW - Enzymatic hydrolysis
KW - Heat-induced gel
KW - Microstructure
KW - Oat protein isolate
KW - Rheology
UR - http://www.scopus.com/inward/record.url?scp=85116062839&partnerID=8YFLogxK
U2 - 10.1016/j.fufo.2021.100053
DO - 10.1016/j.fufo.2021.100053
M3 - Article
AN - SCOPUS:85116062839
SN - 2666-8335
VL - 4
JO - Future Foods
JF - Future Foods
M1 - 100053
ER -