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Functional Colloids from Proteins and Polysaccharides for Food Applications
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Functional Colloids from Proteins and Polysaccharides for Food Applications

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Nutrition".

Deadline for manuscript submissions: closed (28 February 2021) | Viewed by 14218

Special Issue Editor

Prof. Dr.-Ing. Ulrich Kulozik

E-Mail Website
Guest Editor
Technical University of Munich, Chair of Food and Bioprocess Engineering, 85354 Freising, Germany
Interests: food structures; fractionation and separation methods; food preservation; drying methods
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear colleagues,

Biopolymers such as proteins, peptides and polysaccharides have been playing pivotal roles in the structure of food products. Intrinsic molecular functionalities are related to interfacial properties for stabilizing emulsions and foams, gel formation and stabilizing suspensions against the sedimentation of particulate matter. Natural functionalities can be modified in a targeted way by performing related methods of “functionalization” in various compositional environments.

With this Special Issue, we aim at attracting the latest original research and critical review papers from experts worldwide related to bio-colloids in food systems based on natural plant and animal proteins or proteins produced by natural and alternative microbial sources.

Cutting-edge research topics could, for instance, be related to:

  • Creating novel food structures such as aerogels or fibrillar systems;
  • Multiple emulsions or particle-stabilized foams;
  • New and sustainable methods for the fractionation and isolation of bio-colloids from their complex natural environments;
  • Thermal, mechanical and biological processing as tools for functionalization;
  • The interaction of different types of biopolymers in creating structures in complex systems;
  • Analytical methods for characterizing bio-colloidal systems at the microscopic, mesoscopic and macroscopic levels.

Thus, the latest state of the knowledge regarding new methods for food manufacturing and a better mechanistic understanding of structure formation by correlating molecular properties in their various states (native, modified) with structural and functional effects will be made available.

Prof. Dr.-Ing. Ulrich Kulozik
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Foods is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • proteins
  • polysaccharides
  • hydrocolloids
  • biopolymer compatibility
  • multiple emulsions
  • particle-stabilized emulsions
  • aerogels
  • mixed systems
  • structure–function relationships
  • structure analysis

Published Papers (5 papers)

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Research

19 pages, 2416 KiB  
Article
Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins
by David J. Andlinger, Pauline Röscheisen, Claudia Hengst and Ulrich Kulozik
Foods 2021, 10(4), 796; https://doi.org/10.3390/foods10040796 - 08 Apr 2021
Cited by 23 | Viewed by 3932
Abstract
Understanding aggregation in food protein systems is essential to control processes ranging from the stabilization of colloidal dispersions to the formation of macroscopic gels. Patatin rich potato protein isolates (PPI) have promising techno-functionality as alternatives to established proteins from egg white or milk. [...] Read more.
Understanding aggregation in food protein systems is essential to control processes ranging from the stabilization of colloidal dispersions to the formation of macroscopic gels. Patatin rich potato protein isolates (PPI) have promising techno-functionality as alternatives to established proteins from egg white or milk. In this work, the influence of pH and temperature on the kinetics of PPI denaturation and aggregation was investigated as an option for targeted functionalization. At a slightly acidic pH, rates of denaturation and aggregation of the globular patatin in PPI were fast. These aggregates were shown to possess a low amount of disulfide bonds and a high amount of exposed hydrophobic amino acids (S0). Gradually increasing the pH slowed down the rate of denaturation and aggregation and alkaline pH levels led to an increased formation of disulfide bonds within these aggregates, whereas S0 was reduced. Aggregation below denaturation temperature (Td) favored aggregation driven by disulfide bridge formation. Aggregation above Td led to fast unfolding, and initial aggregation was less determined by disulfide bridge formation. Inter-molecular disulfide formation occurred during extended heating times. Blocking different protein interactions revealed that the formation of disulfide bond linked aggregation is preceded by the formation of non-covalent bonds. Overall, the results help to control the kinetics, morphology, and interactions of potato protein aggregation for potential applications in food systems. Full article
(This article belongs to the Special Issue Functional Colloids from Proteins and Polysaccharides for Food Applications)
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17 pages, 1762 KiB  
Article
Assessing Whey Protein Sources, Dispersion Preparation Method and Enrichment of Thermomechanically Stabilized Whey Protein Pectin Complexes for Technical Scale Production
by Jessica M. Filla, Maybritt Stadler, Anisa Heck and Jörg Hinrichs
Foods 2021, 10(4), 715; https://doi.org/10.3390/foods10040715 - 27 Mar 2021
Cited by 5 | Viewed by 2629
Abstract
Whey protein pectin complexes can be applied to replace fat in food products, e.g., pudding and yogurt, contributing to creaminess while adding a source of protein and fiber. Production of these complexes is usually conducted on the laboratory scale in small batches. Recently, [...] Read more.
Whey protein pectin complexes can be applied to replace fat in food products, e.g., pudding and yogurt, contributing to creaminess while adding a source of protein and fiber. Production of these complexes is usually conducted on the laboratory scale in small batches. Recently, a process using a scraped-surface heat exchanger (SSHE) has been employed; however, dispersion preparation time, feasibility of using different whey protein sources and enrichment of the complexes for subsequent drying have not been assessed. Preparing whey protein pectin dispersions by solid mixing of pectin and whey protein powders resulted in larger complexes than powders dispersed separately and subsequently mixed after a hydration time. Dispersions without hydration of the mixed dispersions before thermomechanical treatment had the largest particle sizes. The targeted particle size of d90,3 < 10 µm, an important predictor for creaminess, was obtained for five of the six tested whey protein sources. Dispersions of complexes prepared using whey protein powders had larger particles, with less particle volume in the submicron range, than those prepared using whey protein concentrates. Efficiency of complex enrichment via acid-induced aggregation and subsequent centrifugation was assessed by yield and purity of protein in the pellet and pectin in the supernatant. Full article
(This article belongs to the Special Issue Functional Colloids from Proteins and Polysaccharides for Food Applications)
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15 pages, 10895 KiB  
Article
Double-Network Hydrogels of Corn Fiber Gum and Soy Protein Isolate: Effect of Biopolymer Constituents and pH Values on Textural Properties and Microstructures
by Jinxin Yan, Xin Jia, Wenjia Yan and Lijun Yin
Foods 2021, 10(2), 356; https://doi.org/10.3390/foods10020356 - 07 Feb 2021
Cited by 20 | Viewed by 2529
Abstract
Corn fiber gum (CFG) -soy protein isolate (SPI) double-network (DN) hydrogels were fabricated using laccase and a heat treatment process, in which CFG solution formed the first gel network via laccase oxidation, while SPI formed the second network through heating, as described in [...] Read more.
Corn fiber gum (CFG) -soy protein isolate (SPI) double-network (DN) hydrogels were fabricated using laccase and a heat treatment process, in which CFG solution formed the first gel network via laccase oxidation, while SPI formed the second network through heating, as described in our previous research. The aim of this study was to investigate the influences of CFG/SPI constituents (CFG concentration 0–3%, w/v; SPI concentration 8–10%, w/v) and pH values (5.0–7.5) on the textural properties, microstructures and water-holding capacities (WHC) of the CFG-SPI DN hydrogels. Confocal Laser Scanning Microscopy (CLSM) results showed an apparent phase separation when the CFG concentration was above 1% (w/v). The textural characteristics and WHC of most DN hydrogels were enhanced with increasing concentrations of CFG and SPI. Scanning Electron Microscopy (SEM) observations revealed that the microstructures of DN hydrogels were converted from coarse and irregular to smooth and ordered as pH values increased from 5.0 to 7.5. Excellent textural properties and WHC were observed at pH 7.0. This study developed various CFG-SPI DN hydrogels with diverse textures and structures, governed by the concentrations of protein/polysaccharide and pH values, and also contributes to the understanding of gum–protein interactions in DN hydrogels obtained under different conditions. Full article
(This article belongs to the Special Issue Functional Colloids from Proteins and Polysaccharides for Food Applications)
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14 pages, 7913 KiB  
Article
The Influence of Extrusion Processing on the Gelation Properties of Apple Pomace Dispersions: Involved Cell Wall Components and Their Gelation Kinetics
by Vera Schmid, Heike P. Karbstein and M. Azad Emin
Foods 2020, 9(11), 1536; https://doi.org/10.3390/foods9111536 - 25 Oct 2020
Cited by 7 | Viewed by 2219
Abstract
By-products of fruits and vegetables like apple pomace can serve as techno-functional ingredients in foods. Due to their physicochemical properties, e.g., viscosity, water absorption, or oil-binding, food by-products can modify the texture and sensory perception of products like yogurts and baked goods. It [...] Read more.
By-products of fruits and vegetables like apple pomace can serve as techno-functional ingredients in foods. Due to their physicochemical properties, e.g., viscosity, water absorption, or oil-binding, food by-products can modify the texture and sensory perception of products like yogurts and baked goods. It is known that, by extrusion processing, the properties of by-products can be altered. For example, by thermo-mechanical treatment, the capacity of food by-products to increase viscosity is improved. However, the mechanism and involved components leading to the viscosity increase are unknown. Therefore, the complex viscosity of apple pomace dispersions and the involved fractions as pectin (a major part of the water-soluble fraction), water-soluble and water-insoluble fraction, were measured. In the investigated range, an increase in the pectin yield and water solubility was observed with increasing thermo-mechanical treatment by extrusion processing. However, pectin and water-soluble cell wall components had only a limited effect on the complex viscosity of apple pomace dispersions. The insoluble fraction (particles) were investigated regarding their swelling behavior and influence on the complex viscosity. An intensification of thermo-mechanical treatment resulted in increasing swelling behavior. Full article
(This article belongs to the Special Issue Functional Colloids from Proteins and Polysaccharides for Food Applications)
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14 pages, 1962 KiB  
Article
Influence of Thermomechanical Treatment and Ratio of β-Lactoglobulin and α-Lactalbumin on the Denaturation and Aggregation of Highly Concentrated Whey Protein Systems
by Maria Quevedo, Ulrich Kulozik, Heike P. Karbstein and M. Azad Emin
Foods 2020, 9(9), 1196; https://doi.org/10.3390/foods9091196 - 29 Aug 2020
Cited by 8 | Viewed by 2202
Abstract
The influence of thermomechanical treatment (temperature 60 °C–100 °C and shear rate 0.06 s−1–50 s−1) and mixing ratio of β-lactoglobulin (βLG) and α-lactalbumin (αLA) (5:2 and 1:1) on the denaturation and aggregation of whey protein model systems with a [...] Read more.
The influence of thermomechanical treatment (temperature 60 °C–100 °C and shear rate 0.06 s−1–50 s−1) and mixing ratio of β-lactoglobulin (βLG) and α-lactalbumin (αLA) (5:2 and 1:1) on the denaturation and aggregation of whey protein model systems with a protein concentration of 60% and 70% (w/w) was investigated. An aggregation onset temperature was determined at approx. 80 °C for both systems (5:2 and 1:1 mixing ratio) with a protein concentration of 70% at a shear rate of 0.06 s−1. Increasing the shear rate up to 50 s−1 led to a decrease in the aggregation onset temperature independent of the mixing ratio. By decreasing the protein concentration to 60% in unsheared systems, the aggregation onset temperature decreased compared to that at a protein concentration of 70%. Furthermore, two significantly different onset temperatures were determined when the shear rate was increased to 25 s−1 and 50 s−1, which might result from a shear-induced phase separation. Application of combined thermal and mechanical treatment resulted in overall higher degrees of denaturation independent of the mixing ratio and protein concentration. At the conditions applied, the aggregation of the βLG and αLA mixtures was mainly due to the formation of non-covalent bonds. Although the proportion of disulfide bond aggregation increased with treatment temperature and shear rate, it was higher at a mixing ratio of 5:2 compared to that at 1:1. Full article
(This article belongs to the Special Issue Functional Colloids from Proteins and Polysaccharides for Food Applications)
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