Editorial

4 pages, 194 KiB

Open AccessEditorial

Processing Effects on Protein Structure and Physicochemical Properties

by Vibeke Orlien and Åsmund Rinnan

Foods 2022, 11(11), 1607; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11111607 - 30 May 2022

Cited by 1 | Viewed by 1542

Raw materials, whether it is from the animal or plant kingdom, undergo some kind of (domestic or industrial) processing prior to consumption [...] Full article

(This article belongs to the Special Issue Processing Effects on Protein Structure and Physicochemical Properties)

Research

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11 pages, 12588 KiB

Open AccessArticle

Gluten Conformation at Different Temperatures and Additive Treatments

by Pavalee Chompoorat, Ayuba Fasasi, Barry K. Lavine and Patricia Rayas-Duarte

Foods 2022, 11(3), 430; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11030430 - 01 Feb 2022

Cited by 4 | Viewed by 1618

Abstract

The effect of temperature (25, 45, and 65 °C) on the gluten secondary structure was investigated by using Fourier transform infrared (FTIR) spectroscopy and modulation of disulfide and hydrogen bonds contributions (100 ppm ascorbic acid (AA), 0.6% diacetyl tartaric acid ester of monoglycerides [...] Read more.

The effect of temperature (25, 45, and 65 °C) on the gluten secondary structure was investigated by using Fourier transform infrared (FTIR) spectroscopy and modulation of disulfide and hydrogen bonds contributions (100 ppm ascorbic acid (AA), 0.6% diacetyl tartaric acid ester of monoglycerides (DATEM), and 0.25 mM dithiothreitol (DTT)). The results showed that additives heated at 65 °C altered most of the gluten matrix formation by changing structural secondary structures compared to the secondary structures of native gluten (control). The content of random coils, α-helices, and β-sheet of gluten increased, while the extent of β-turns and antiparallel β-sheets decreased, which led to the transformation to a more stable secondary conformation. In addition, the rheological properties (%creep strain) revealed that gluten deformation increased during the heating process with all of the additives. The chemometric method could quantitate an overall alteration of gluten polymerization and gluten matrix formation during heating with additive treatments. Full article

(This article belongs to the Special Issue Processing Effects on Protein Structure and Physicochemical Properties)

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19 pages, 1921 KiB

Open AccessEditor’s ChoiceArticle

Effect of the Post-Harvest Processing on Protein Modification in Green Coffee Beans by Phenolic Compounds

by Gustavo A. Figueroa Campos, Johannes G. K. T. Kruizenga, Sorel Tchewonpi Sagu, Steffen Schwarz, Thomas Homann, Andreas Taubert and Harshadrai M. Rawel

Foods 2022, 11(2), 159; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11020159 - 08 Jan 2022

Cited by 10 | Viewed by 3568

Abstract

The protein fraction, important for coffee cup quality, is modified during post-harvest treatment prior to roasting. Proteins may interact with phenolic compounds, which constitute the major metabolites of coffee, where the processing affects these interactions. This allows the hypothesis that the proteins are [...] Read more.

The protein fraction, important for coffee cup quality, is modified during post-harvest treatment prior to roasting. Proteins may interact with phenolic compounds, which constitute the major metabolites of coffee, where the processing affects these interactions. This allows the hypothesis that the proteins are denatured and modified via enzymatic and/or redox activation steps. The present study was initiated to encompass changes in the protein fraction. The investigations were limited to major storage protein of green coffee beans. Fourteen Coffea arabica samples from various processing methods and countries were used. Different extraction protocols were compared to maintain the status quo of the protein modification. The extracts contained about 4–8 µg of chlorogenic acid derivatives per mg of extracted protein. High-resolution chromatography with multiple reaction monitoring was used to detect lysine modifications in the coffee protein. Marker peptides were allocated for the storage protein of the coffee beans. Among these, the modified peptides K.FFLANGPQQGGK.E and R.LGGK.T of the α-chain and R.ITTVNSQK.I and K.VFDDEVK.Q of β-chain were detected. Results showed a significant increase (p < 0.05) of modified peptides from wet processed green beans as compared to the dry ones. The present study contributes to a better understanding of the influence of the different processing methods on protein quality and its role in the scope of coffee cup quality and aroma. Full article

(This article belongs to the Special Issue Processing Effects on Protein Structure and Physicochemical Properties)

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15 pages, 3461 KiB

Open AccessArticle

Effects of Freeze–Thaw Cycles on Water Migration, Microstructure and Protein Oxidation in Cuttlefish

by Ying Lv and Jing Xie

Foods 2021, 10(11), 2576; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10112576 - 26 Oct 2021

Cited by 17 | Viewed by 2666

Abstract

This study was conducted to analyze the effects of multiple freeze–thaw (F-T) cycles on microstructural disruption, water migration, protein oxidation and textural properties of cuttlefish. Low-field nuclear magnetic resonance (LF-NMR) showed an increase in the proportion of free water in cuttlefish flesh. It [...] Read more.

This study was conducted to analyze the effects of multiple freeze–thaw (F-T) cycles on microstructural disruption, water migration, protein oxidation and textural properties of cuttlefish. Low-field nuclear magnetic resonance (LF-NMR) showed an increase in the proportion of free water in cuttlefish flesh. It was also observed by scanning electron microscopy (SEM) that multiple F-T cycles increased the gap between muscle fibers and disrupted the original intact and compact structure. The results of Fourier transform infrared spectroscopy, intrinsic fluorescence spectroscopy, Ca²⁺ATPase content, sulfhydryl content and free amino acid content indirectly prove that multiple F-T cycles can lead to the destruction of the a-helical structure of cuttlefish myofibril protein and the content of irregular curls increased, protein aggregation and degradation, and tryptophan oxidation. In addition, after repeated freezing and thawing, the water holding capacity, whiteness value, elasticity and chewiness of cuttlefish flesh decreased, the total volatile base nitrogen content increased. It can be concluded that the freeze–thaw cycles are very harmful to the quality of the frozen foods, so it is important to keep the temperature stable in the low-temperature food logistics. Full article

(This article belongs to the Special Issue Processing Effects on Protein Structure and Physicochemical Properties)

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11 pages, 1039 KiB

Open AccessCommunication

Two Statistical Tools for Assessing Functionality and Protein Characteristics of Different Fava Bean (Vicia faba L.) Ingredients

by Siddharth Sharan, Jens Zotzel, Johannes Stadtmüller, Daniel Bonerz, Julian Aschoff, Anne Saint-Eve, Marie-Noëlle Maillard, Karsten Olsen, Åsmund Rinnan and Vibeke Orlien

Foods 2021, 10(10), 2489; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10102489 - 18 Oct 2021

Cited by 7 | Viewed by 3090

Abstract

Fava bean (Vicia faba L.) is a promising source of proteins that can be potentially used as nutritional and/or functional agents for industrial food applications. Fava ingredients are industrially produced, modified, and utilized for food applications. Their processing conditions influence physico-chemical protein [...] Read more.

Fava bean (Vicia faba L.) is a promising source of proteins that can be potentially used as nutritional and/or functional agents for industrial food applications. Fava ingredients are industrially produced, modified, and utilized for food applications. Their processing conditions influence physico-chemical protein properties that further impact ingredient functionality. To design a functionally suitable ingredient, an understanding of the interrelationships between different properties is essential. Hence, this work aimed to assess two statistical analytical tools, Pearson’s correlation and Principal Component Analysis (PCA), for investigating the role of the process conditions of fava ingredients on their functional and protein properties. Fava concentrates were processed by pH (2, 4, 6.4 and 11), temperature (55, 75 and 95

^{\circ}

C) and treatment duration (30 and 360 min) into different modified ingredients. These were utilized under two application conditions (pH 4 and 7), and their foam and emulsion properties as well as their ingredient characteristics (charge, solubility, and intrinsic fluorescence) were measured. The results show that foam and emulsion properties are not correlated to each other. They are associated with different protein and non-protein attributes as fava concentrate is a multi-component matrix. Importantly, it is found that the results from the two statistical tools are not fully comparable but do complement each other. This highlights that both statistical analytical tools are equally important for a comprehensive understanding of the impact of process conditions on different properties and the interrelationships between them. Therefore, it is recommended to use Pearson’s correlation and principal component analysis in future investigations of new plant-based proteins. Full article

(This article belongs to the Special Issue Processing Effects on Protein Structure and Physicochemical Properties)

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11 pages, 1212 KiB

Open AccessArticle

Effect of Protein Denaturation Temperature on Rheological Properties of Baltic Herring (Clupea harengus membras) Muscle Tissue

by Agnieszka Strzelczak, Jerzy Balejko, Mariusz Szymczak and Agata Witczak

Foods 2021, 10(4), 829; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10040829 - 11 Apr 2021

Cited by 14 | Viewed by 3270

Abstract

The technological properties of raw fish are influenced by the changes in protein structure under heating, which determines the texture and quality of the product. The aim of the study was to examine the protein denaturation temperature and the rheological properties of Baltic [...] Read more.

The technological properties of raw fish are influenced by the changes in protein structure under heating, which determines the texture and quality of the product. The aim of the study was to examine the protein denaturation temperature and the rheological properties of Baltic herring muscle tissue. The thermal properties were determined by the differential scanning calorimetry (DSC) method and the rheological properties were determined using dynamic oscillatory tests. DSC showed four peaks associated with denaturing transformations of myosin (39.59 °C), sarcoplasm (51.67 °C), connective tissue (63.16 °C), and actin (74.40 °C). Analysis showed that not all transformations occurred according to the same kinetic model. The first two and the last peak are described by 1st order kinetics, while peak 3 is described by 2nd order kinetics. Correlating the changes in fish tissue structure during heating with the rheological characteristics provides more information. The obtained kinetics models correlated very strongly with the results of model testing. Rheological changes of the G’ and G” values had two inflexion points and demonstrate a high degree of convergence with the DSC changes of herring muscle tissue from 20 to 85 °C. Full article

(This article belongs to the Special Issue Processing Effects on Protein Structure and Physicochemical Properties)

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13 pages, 2091 KiB

Open AccessArticle

Water Absorption Capacity Determines the Functionality of Vital Gluten Related to Specific Bread Volume

by Marina Schopf and Katharina Anne Scherf

Foods 2021, 10(2), 228; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10020228 - 23 Jan 2021

Cited by 18 | Viewed by 7606

Abstract

Vital gluten is often used in baking to supplement weak wheat flours and improve their baking quality. Even with the same recipe, variable final bread volumes are common, because the functionality differs between vital gluten samples also from the same manufacturer. To understand [...] Read more.

Vital gluten is often used in baking to supplement weak wheat flours and improve their baking quality. Even with the same recipe, variable final bread volumes are common, because the functionality differs between vital gluten samples also from the same manufacturer. To understand why, the protein composition of ten vital gluten samples was investigated as well as their performance in a microbaking test depending on the water content in the dough. The gluten content and composition as well the content of free thiols and disulfide bonds of the samples were similar and not related to the specific bread volumes obtained using two dough systems, one based on a baking mixture and one based on a weak wheat flour. Variations of water addition showed that an optimal specific volume of 1.74–2.38 mL/g (baking mixture) and 4.25–5.49 mL/g (weak wheat flour) was reached for each vital gluten sample depending on its specific water absorption capacity. Full article

(This article belongs to the Special Issue Processing Effects on Protein Structure and Physicochemical Properties)

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Review

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18 pages, 1281 KiB

Open AccessReview

Survey on Methods for Investigating Protein Functionality and Related Molecular Characteristics

by Yuqi Zhang, Siddharth Sharan, Åsmund Rinnan and Vibeke Orlien

Foods 2021, 10(11), 2848; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10112848 - 18 Nov 2021

Cited by 22 | Viewed by 3608

Abstract

Proteins from various sources are widely used in the food industry due to their unique functional performances in food products. The functional properties of proteins are somehow dictated by their molecular characteristics, but the exact relationship is not fully understood. This review gives [...] Read more.

Proteins from various sources are widely used in the food industry due to their unique functional performances in food products. The functional properties of proteins are somehow dictated by their molecular characteristics, but the exact relationship is not fully understood. This review gives a tangible overview of the methods currently available for determining protein functionality and related molecular characteristics in order to support further research on protein ingredients. The measurements of protein functionality include solubility, water holding capacity, oil holding capacity, emulsion property, foam property, and gelation. This review also provides a description of different methods of molecular characteristics including electrophoresis, surface hydrophobicity and charge, molecular interaction, and thermal property measurement. Additionally, we have put significant emphasis on spectroscopic methods (ultraviolet-visible, Fourier transform infrared, Raman, circular dichroism, fluorescence and nuclear magnetic resonance). In conclusion, first and foremost, there is a need to agree on a standardization of the analytical methods for assessing functional properties. Moreover, it is mandatory to couple different analyses of molecular characteristics to measure and monitor the structural changes obtained by different processing methods in order to gain knowledge about the relationship with functionality. Ideally, a toolbox of protein analytical methods to measure molecular characteristics and functionality should be established to be used in a strategic design of protein ingredients. Full article

(This article belongs to the Special Issue Processing Effects on Protein Structure and Physicochemical Properties)

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20 pages, 1410 KiB

Open AccessReview

Methods for the Modification and Evaluation of Cereal Proteins for the Substitution of Wheat Gluten in Dough Systems

by Javier Espinoza-Herrera, Luz María Martínez, Sergio O. Serna-Saldívar and Cristina Chuck-Hernández

Foods 2021, 10(1), 118; https://0-doi-org.brum.beds.ac.uk/10.3390/foods10010118 - 08 Jan 2021

Cited by 14 | Viewed by 6066

Abstract

The substitution of wheat gluten in the food industry is a relevant research area because the only known treatment for celiac disease is abstinence from this protein complex. The use of gluten-free cereals in dough systems has demonstrated that the viscoelastic properties of [...] Read more.

The substitution of wheat gluten in the food industry is a relevant research area because the only known treatment for celiac disease is abstinence from this protein complex. The use of gluten-free cereals in dough systems has demonstrated that the viscoelastic properties of gluten cannot be achieved without the modification of the protein fraction. The quality of the final product is determined by the ability of the modification to form a matrix similar to that of gluten and to reach this, different methods have been proposed and tested. These procedures can be classified into four main types: chemical, enzymatic, physical, and genetic. This article provides a comprehensive review of the most recent research done in protein modification of cereal and pseudocereals for gluten substitution. The reported effects and methodologies for studying the changes made with each type of modification are described; also, some opportunity areas for future works regarding the study of the effect of protein modifications on gluten-free products are presented. Full article

(This article belongs to the Special Issue Processing Effects on Protein Structure and Physicochemical Properties)

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