scholarly journals Interaction of whey protein with polyphenols from salal fruits ( Gaultheria shallon ) and the effects on protein structure and hydrolysis pattern by Flavourzyme ®

2019 ◽  
Vol 55 (3) ◽  
pp. 1281-1288 ◽  
Author(s):  
He Ni ◽  
Helen Hayes ◽  
David Stead ◽  
Guang Liu ◽  
Huaijie Yang ◽  
...  
Keyword(s):  
Protein Structure ◽  
Whey Protein ◽  
Gaultheria Shallon

scholarly journals Production of ACE Inhibitory Peptides from Whey Proteins Modified by High Intensity Ultrasound Using Bromelain

Foods ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 2099
Author(s):  
Lucía Abadía-García ◽  
Eduardo Castaño-Tostado ◽  
Anaberta Cardador-Martínez ◽  
Sandra Teresita Martín-del-Campo ◽  
Silvia L. Amaya-Llano
Keyword(s):  
Protein Structure ◽  
Enzymatic Hydrolysis ◽  
Whey Protein ◽  
High Intensity ◽  
Whey Proteins ◽  
High Intensity Ultrasound ◽  
Peptide Profile ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

High Intensity Ultrasound (HIUS) can induce modification of the protein structure. The combination of enzymatic hydrolysis and ultrasound is an interesting strategy to improve the release of the Angiotensin-Converting Enzyme (ACE) inhibitory peptides. In this study, whey proteins were pretreated with HIUS at two levels of amplitude (30 and 50%) for 10 min, followed by hydrolysis using the vegetable protease bromelain. The hydrolysates obtained were ultrafiltrated and their fractions were submitted to a simulated gastrointestinal digestion. The conformational changes induced by HIUS on whey proteins were analyzed using Fourier-transform infrared spectroscopy by attenuated total reflectance (FTIR-ATR) and intrinsic spectroscopy. It was found that both levels of ultrasound pretreatment significantly decreased the IC50 value (50% Inhibitory Concentration) of the hydrolysates in comparison with the control (α = 0.05). After this treatment, HIUS-treated fractions were shown as smaller in size and fractions between 1 and 3 kDa displayed the highest ACE inhibition activity. HIUS promoted significant changes in whey protein structure, inducing, unfolding, and aggregation, decreasing the content of α-helix, and increasing β-sheets structures. These findings prove that ultrasound treatment before enzymatic hydrolysis is an innovative and useful strategy that modifies the peptide profile of whey protein hydrolysates and enhances the production of ACE inhibitory peptides.

Isoenergic modification of whey protein structure by denaturation and crosslinking using transglutaminase

2018 ◽  
Vol 9 (2) ◽  
pp. 797-805 ◽  
Author(s):  
Emil G. P. Stender ◽  
Glykeria Koutina ◽  
Kristoffer Almdal ◽  
Tue Hassenkam ◽  
Alan Mackie ◽  
...  
Keyword(s):  
Protein Structure ◽  
Whey Protein ◽  
Structural Effect

The structural effect of denaturation of whey protein by heat or pH and subsequent crosslinking by transglutaminase.

Immunoprobes for thermally-induced alterations in whey protein structure and their application to the analysis of thermally-treated milks

2003 ◽  
Vol 15 (2) ◽  
pp. 77-91 ◽  
Author(s):  
Ludmila Karamonová ◽  
Ladislav Fukal ◽  
Milan Kodíček ◽  
Pavel Rauch ◽  
E. N. Clare Mills ◽  
...  
Keyword(s):  
Protein Structure ◽  
Whey Protein ◽  
Thermally Induced ◽  
Thermally Treated

scholarly journals The Effect of Atmospheric Plasma on a Protein Thermal Shift Assay of Powdered Whey Protein Isolate

2018 ◽  
Author(s):  
Danielle Aguilar
Keyword(s):  
Protein Structure ◽  
Whey Protein ◽  
Structural Changes ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Inorganic Materials ◽  
Atmospheric Plasma ◽  
Food Ingredient ◽  
Thermal Shift Assay ◽  
Thermal Shift

Whey is both a dietary supplement as well as a food ingredient. It is a byproduct of the cheese making process, and it can be processed further to create three forms, namely whey isolate, whey concentrate and whey hydrolysate. Given whey’s complexity and applicability in the food, nutrition and health industries, understanding how changes to its structure contribute to or affect its function is of great interest. One method by which protein structure could be altered is via plasma-surface modification (PSM), an effective surface altering technique of inorganic materials, and there is growing interest in its application on organic materials such as proteins. However, research on the use of PSM to promote structural changes of food proteins has been limited as studies have mostly focused on aqueous solutions and their contributions to pharmacological development. The purpose of this study is to investigate whether the structure of dry powdered whey protein isolate can be modified by atmospheric plasma. The Protein Thermal Shift Assay (PTSA) was implemented to measure structural changes of PSM altered whey protein powder, and a range of protein structure alterations was observed, with a highest total change of 12.77% between control and treated protein. The applicability of changes in protein structure via atmospheric plasma could have several economical and nutritional benefits as it could be implemented in the process of whey product optimization, which in turn could be of use in the food and nutrition sectors.

scholarly journals Ohmic heating for the dairy industry: a potential technology to develop probiotic dairy foods in association with modifications of whey protein structure

2018 ◽  
Vol 22 ◽  
pp. 95-101 ◽  
Author(s):  
Ricardo Nuno Pereira ◽  
José António Teixeira ◽  
António Augusto Vicente ◽  
Leandro Pereira Cappato ◽  
Marcus Vinicius da Silva Ferreira ◽  
...  
Keyword(s):  
Protein Structure ◽  
Whey Protein ◽  
Ohmic Heating ◽  
Dairy Industry ◽  
Dairy Foods
Sign in / Sign up

Export Citation Format

Share Document