Structural and Nutritional Characterization of Food Proteins and Polysaccharides

A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Physics and (Bio)Chemistry".

Deadline for manuscript submissions: closed (20 June 2020) | Viewed by 12389

Special Issue Editors


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Guest Editor
MTT Agrifood Research Finland, Biotechnology and Food Research, Alimentum, FI-31600 Jokioinen, Finland
Interests: foods, dairy, milk and plant proteins, peptides, analytical methods

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Guest Editor
Department of Chemistry, Biotechnology and Food Science (IKBM), Norwegian University of Life Sciences (NMBU), Oslo, Norway
Interests: food lipid, meat, food nutrition, food science

Special Issue Information

Dear Colleagues,

Sourcing and providing proteins are crucial in feeding the world and the global need for proteins will increase steeply along with population growth. Proteins provide energy, but additionally have a wide range of functions from enzymatic activities in the body to health beneficial attributes. Furthermore, proteins play an important role in food manufacture and often provide the binding, water- or oil-holding, emulsifying, foaming or other functional attributes required to ensure optimum sensory and taste benefits for the consumer. Polysaccharides from plants have been utilised by the food industry for many years as gums and stabilising agents and can mediate carbohydrate digestion and thus manipulate the nutritional quality of foods. This is especially the case in the context of polysaccharides affecting postprandial blood glucose levels, obesity, diabetes, and even neuro-degenerative diseases. The purpose of this issue is to highlight current and new protein and polysaccharide sources and their associated functional, nutritional qualities.

Dr. Anne Pihlanto
Dr. Tove Gulbrandsen Devold
Guest Editors

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Keywords

  • Chemistry and characterization
  • Functional properties
  • Nutritional value
  • Application
  • Interactions
  • Protein
  • Polysaccharide
  • Antinutrients
  • Beneficial compounds

Published Papers (3 papers)

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Research

11 pages, 836 KiB  
Article
β-Cyclodextrin-Mediated Beany Flavor Masking and Textural Modification of an Isolated Soy Protein-Based Yuba Film
by Eun-Jung Lee, Honggyun Kim, Jong Yeop Lee, Karna Ramachandraiah and Geun-Pyo Hong
Foods 2020, 9(6), 818; https://doi.org/10.3390/foods9060818 - 22 Jun 2020
Cited by 20 | Viewed by 4084
Abstract
The application of β-cyclodextrin (CD) to remove unattractive volatile compounds has been applied in various food products. This study investigated the effect of CD concentration (1–4%) on the beany flavor masking and textural modification of yuba film prepared by isolated soy protein (ISP) [...] Read more.
The application of β-cyclodextrin (CD) to remove unattractive volatile compounds has been applied in various food products. This study investigated the effect of CD concentration (1–4%) on the beany flavor masking and textural modification of yuba film prepared by isolated soy protein (ISP) in the presence of (+CD), or after removing, the flavor-entrapped CD (−CD). Based on gas chromatography–mass spectrometry (GC–MS), the addition of CD caused a decrease in 1-octen-3-ol, benzaldehyde, hexanal, and 2-heptanone, which are characterized as the major beany flavor compounds. Regardless of presence or removal, the use of CD was effective in reducing beany flavor in yuba film. Scanning electron microscopy (SEM) observation indicated that the CD present in yuba film was distributed on the lower surface and matrices of the films. In yuba film containing 4% CD, the CD crystals were concentrated on both the upper and lower surfaces of the film. The textural properties of the yuba film were affected by the presence or removal of CD, and better puncture strength was obtained when yuba was made after removing the CD. Therefore, this study indicates that the addition of CD was a good approach to mask the beany flavor of soy protein-based products, and textural properties could be improved by removing CD from the product formulation. Full article
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16 pages, 1396 KiB  
Article
Physicochemical Characteristics of Protein Isolated from Thraustochytrid Oilcake
by Thi Linh Nham Tran, Ana F. Miranda, Aidyn Mouradov and Benu Adhikari
Foods 2020, 9(6), 779; https://doi.org/10.3390/foods9060779 - 11 Jun 2020
Cited by 14 | Viewed by 3923
Abstract
The oil from thraustochytrids, unicellular heterotrophic marine protists, is increasingly used in the food and biotechnological industries as it is rich in omega-3 fatty acids, squalene and a broad spectrum of carotenoids. This study showed that the oilcake, a by-product of oil extraction, [...] Read more.
The oil from thraustochytrids, unicellular heterotrophic marine protists, is increasingly used in the food and biotechnological industries as it is rich in omega-3 fatty acids, squalene and a broad spectrum of carotenoids. This study showed that the oilcake, a by-product of oil extraction, is equally valuable as it contained 38% protein/dry mass, and thraustochytrid protein isolate can be obtained with 92% protein content and recovered with 70% efficiency. The highest and lowest solubilities of proteins were observed at pH 12.0 and 4.0, respectively, the latter being its isoelectric point. Aspartic acid, glutamic acid, histidine, and arginine were the most abundant amino acids in proteins. The arginine-to-lysine ratio was higher than one, which is desired in heart-healthy foods. The denaturation temperature of proteins ranged from 167.8–174.5 °C, indicating its high thermal stability. Proteins also showed high emulsion activity (784.1 m2/g) and emulsion stability (209.9 min) indices. The extracted omega-3-rich oil melted in the range of 30–34.6 °C and remained stable up to 163–213 °C. This study shows that thraustochytrids are not only a valuable source of omega 3-, squalene- and carotenoid-containing oils, but are also rich in high-value protein with characteristics similar to those from oilseeds. Full article
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13 pages, 895 KiB  
Article
Enhanced Solubility of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation
by Hristo Kalaydzhiev, Radoslav Georgiev, Petya Ivanova, Magdalena Stoyanova, Cristina L. M. Silva and Vesela I. Chalova
Foods 2020, 9(6), 703; https://doi.org/10.3390/foods9060703 - 1 Jun 2020
Cited by 25 | Viewed by 3969
Abstract
The solubility of plant protein isolates is a key determinant of their potential application. Two protein isolates (PI) from ethanol-treated industrial rapeseed meal, PI10.5–2.5 and PI2.5–8.5, were prepared by sequential isoelectric precipitation of alkali-extracted proteins (pH 12) starting from pH [...] Read more.
The solubility of plant protein isolates is a key determinant of their potential application. Two protein isolates (PI) from ethanol-treated industrial rapeseed meal, PI10.5–2.5 and PI2.5–8.5, were prepared by sequential isoelectric precipitation of alkali-extracted proteins (pH 12) starting from pH 10.5 to 2.5 or from pH 2.5 to 8.5, respectively. Biochemical analyses revealed that PI2.5–8.5 contained a higher amount of crude protein (72.84%) than PI10.5–2.5 (68.67%). In the same protein isolate, the level of total phenols (0.71%) was almost two-fold higher than that in PI10.5–2.5 (0.42%). No glucosinolates were established in both protein isolates. SDS-PAGE analysis demonstrated that PI10.5–2.5 contained 10 to 15 kDa protein fractions in a relatively higher amount, while PI2.5–8.5 was enriched in 18 to 29 kDa protein fractions. PI10.5–2.5 exhibited high solubility, varying from 41.74% at pH 4.5 to 65.13% at pH 6.5, while PI2.5–8.5 was almost two-fold less soluble under the same conditions. Up to pH 5.5, the addition of NaCl at 0.03 and 0.25 M diminished the solubility of PI2.5–8.5, while the solubility of PI10.5–2.5 was increased. The supplementation of PI10.5–2.5 with 0.25 M NaCl enhanced the protein solubility to 56.11% at pH 4.5 and 94.26% at pH 6.5. The addition of 0.03 M NaCl also increased the solubility of this protein isolate but to a lower extent. Overall, the approach for sequential precipitation of proteins influenced the biochemical characteristics, protein fractional profile and solubility of prepared protein isolates. Full article
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