11 results match your criteria: "Aarhus University Centre for Innovative Food Research[Affiliation]"

During processing and storage of both conventional and lactose-hydrolyzed UHT milk (LHM), aggregation of milk proteins occurs. Protein aggregation can inter alia occur via nonreducible covalent cross-links derived from either Maillard or dehydroalanine (DHA) pathways. To study this further in relation to processing method and lactase enzyme purity, LHM was produced using 3 different lactase preparations, with lactase enzymes added in a dairy setting either before (prehydrolysis) or after (posthydrolysis) UHT treatment.

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Stability of R-phycoerythrin from Furcellaria lumbricalis - Dependence on purification strategies and purity.

Food Res Int

August 2024

Department of Food Science, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark; CBIO, Aarhus University Centre for Circular Bioeconomy, 8830 Tjele, Denmark; CiFOOD, Aarhus University Centre for Innovative Food Research, 8000 Aarhus C, Denmark. Electronic address:

R-phycoerythrin (R-PE) is the most abundant, naturally occurring phycobiliproteins found in red algae. The spectroscopic and structural properties of phycobiliproteins exhibit unique absorption characteristics with two significant absorption maxima at 498 and 565 nm, indicating two different chromophores of R-PE, phycourobilin and phycoerythrobilin respectively. This study aimed to clarify how the stability of R-PE purified from F.

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Stability of individual anthocyanins from black carrots stored in light and darkness - Impact of acylation.

Food Res Int

June 2024

Department of Food Science, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark; CBIO, Aarhus University Centre for Circular Bioeconomy, 8830 Tjele, Denmark; CiFOOD, Aarhus University Centre for Innovative Food Research, 8200 Aarhus N, Denmark. Electronic address:

Black carrot anthocyanins have gained increasing attention as natural coloring agent, owing to their higher stability than anthocyanins from berries. The stability has been attributed to their higher degree of acylation. This study investigated the impact of acylation on the stability of individual anthocyanins during storage in light and darkness.

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In vitro protein digestibility of RuBisCO from alfalfa obtained from different processing histories: Insights from free N-terminal and mass spectrometry study.

Food Chem

February 2024

Department of Food Science, Faculty of Technical Sciences, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark; CiFOOD Aarhus University Centre for Innovative Food Research, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark; CBIO Aarhus University Centre for Circular Bioeconomy, Aarhus University, Blichers Allé 20, 8830 Tjele, Denmark. Electronic address:

Ribulose-1,5-bisphosphate-carboxylase/oxygenase (RuBisCO) from alfalfa is a potentially climate-friendly alternative protein with a promising amino acid composition. The balance between yield and purity is a challenge for alternative plant proteins, partly due to the naturally occurring antinutrients. Therefore, measuring the in vitro protein digestibility (IVPD) of RuBisCO with various purity levels is of interest.

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There is a growing need for protein for both feed and food in order to meet future demands. It is imperative to explore and utilize novel protein sources such as protein from leafy plant material, which contains high amounts of the enzyme ribulose-1,5-biphosphate carboxylase/oxygenase (RuBisCo). Leafy crops such as grasses and legumes can in humid climate produce high protein yields in a sustainable way when compared with many traditional seed protein crops.

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Mechanisms behind protein-protein interactions in a β-lg-legumin co-precipitate.

Food Chem

March 2022

Aarhus University, Department of Food Science, Agro Food Park 48, 8200 Aarhus N, Denmark; CiFOOD, Aarhus University Centre for Innovative Food Research, 8200 Aarhus N, Denmark; CBIO, Aarhus University Centre for Circular Bioeconomy, 8800 Tjele, Denmark. Electronic address:

Interactions between pea protein and whey protein isolates in co-precipitates and blends consist of a combination of disulphide bonds, hydrophobic and electrostatic interactions. The present study aims to clarify if the two proteins with free thiols, β-lactoglobulin (β-lg) and legumin, played a significant role for these interactions. This study used different reagents to modify the conditions of interactions: N-ethylmaleimide (NEM) was used to block reactive thiols, while NaCl and SDS were used to prevent electrostatic or hydrophobic interactions, respectively.

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Aging is the most critical factor that influences the quality of post-ovulatory oocytes. Age-related molecular pathways remain poorly understood in fish oocytes. In this study, we examined the effect of oocyte aging on specific histone acetylation in common carp .

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Food contact materials (FCM) are defined as the objects and materials intended to come into direct or indirect contact with foodstuff, while food contact articles are defined as objects, being equipment, containers, packaging and various utensils which are clearly intended to be used for the manufacture, preparation, conservation, flow, transport or handling of foodstuffs [...

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Our objective was to determine the content of the bioactive protein osteopontin (OPN) in bovine milk and identify factors influencing its concentration. OPN is expressed in many tissues and body fluids, with by far the highest concentrations in milk. OPN plays a role in immunological and developmental processes and it has been associated with several milk production traits and lactation persistency in cows.

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For potato proteins to be used as a food ingredient, the level of natural potato defense substances, the glycoalkaloids (GAs), should be limited. In this work, a method is developed for quantification of the two major potato GAs, α-solanine and α-chaconine, as well as for their aglycon form, solanidine, using liquid chromatography-mass spectrometry single quadrupole in single ion monitoring mode. Standard solutions of GA and a food-grade potato protein powder was used to validate the method.

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Mechanism behind the degradation of aqueous norbixin upon storage in light and dark environment.

Food Chem

April 2020

Department of Food Science, Aarhus University, Agro Food Park 48, 8200 Aarhus N, Denmark; CBIO, Aarhus University Centre for Circular Bioeconomy, 8000 Aarhus C, Denmark; iFOOD, Aarhus University Centre for Innovative Food Research, 8000 Aarhus C, Denmark. Electronic address:

Buffered aqueous solutions of norbixin were stored in light and dark, and analyzed using mass spectrometry. Compounds with both higher and lower masses than norbixin were detected, suggesting the formation of oxidation products and oxidative cleavage products of norbixin. The norbixin oxidation products included compounds containing several oxidations.

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