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Food By-Products as a Source of Proteins and Peptides
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Food By-Products as a Source of Proteins and Peptides

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

Deadline for manuscript submissions: closed (15 February 2022) | Viewed by 18491

Special Issue Editor

Dr. Maria Hayes

E-Mail Website
Guest Editor
The Food BioSciences Department, Teagasc Food Research Centre, Ashtown, Dublin 15, Ireland
Interests: proteins; peptides; bioactives; animal health; functional foods; heart health; diabetes; inflammation; pain; pharma; functional foods
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Processing foods generates co-products and by-products that can be rich in proteins and peptides that are largely not utilised at present. To make food processing more economically and environmentally sustainable, procedures can be implemented that target total use of the biomass and go towards generating new markets and products. These products often consist of protein and peptides that have several potential techno-functional and bioactive health benefits. Nutritional benefits and methods to measure the same will be collated. This Special Issue will look at the generation of proteins and bioactive peptides from several food sources including traditional sources such as meat, dairy and fish but also their co-products. In addition, extraction and characterisation of proteins and peptides from alternative protein sources including cereals, microalgae, seaweeds and their by-products of extraction will also be examined. Techno-functional characterisation and life cycle analysis will be discussed along with current and potential applications of products developed from food processing by-products.

Dr. Maria Hayes
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

  • by-product proteins
  • bioactive peptides for health
  • legislation
  • microalgae
  • seaweed protein
  • co-products of extraction
  • heart health
  • mental health
  • metabolic syndrome
  • sarcopenia
  • weight gain/loss
  • life cycle analysis
  • preventative healthcare
  • fish, marine peptides
  • meat and dairy
  • cereals
  • product carbon footprint

Published Papers (6 papers)

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Research

16 pages, 6373 KiB  
Article
Recovery of Functional Proteins from Pig Brain Using pH-Shift Processes
by Jaruwan Chanted, Worawan Panpipat, Ling-Zhi Cheong and Manat Chaijan
Foods 2022, 11(5), 695; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11050695 - 26 Feb 2022
Cited by 2 | Viewed by 1572
Abstract
The goal of this work is to explore if pH-shift processing could be used as a cold refinery technique to manufacture pig brain protein isolate (PI). Pig brain protein had the highest solubility at pH 2 (acid method) and pH 12 (alkaline method). [...] Read more.
The goal of this work is to explore if pH-shift processing could be used as a cold refinery technique to manufacture pig brain protein isolate (PI). Pig brain protein had the highest solubility at pH 2 (acid method) and pH 12 (alkaline method). As the protein solution’s zeta-potential was near 0 with the lowest solubility, pH 5.0 was chosen as the precipitation pH. Alkaline process produced a 32% dry matter yield with phospholipid content of 35 mg/100 g. The alkaline-made PI was better at forming soft gels and had good emulsifying and foaming capabilities. Although the acid-made PI included less residual lipid and total haem protein and was whiter in colour, it could not be gelled. Acid-made PI was more prone to lipid oxidation with a poorer ability to function as an emulsifier and foaming agent. Thus, functional proteins from pig brain may be isolated using the alkaline pH-shift technique. Full article
(This article belongs to the Special Issue Food By-Products as a Source of Proteins and Peptides)
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18 pages, 22257 KiB  
Article
Tyrosinase Inhibitory and Antioxidant Activity of Enzymatic Protein Hydrolysate from Jellyfish (Lobonema smithii)
by Maytamart Upata, Thanyaporn Siriwoharn, Sakunkhun Makkhun, Suthasinee Yarnpakdee, Joe M. Regenstein and Sutee Wangtueai
Foods 2022, 11(4), 615; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11040615 - 21 Feb 2022
Cited by 22 | Viewed by 2960
Abstract
The optimization of antioxidant and anti-tyrosinase activity during jellyfish hydrolysate preparation was studied using a response surface methodology (RSM) with a face-centered composite design. The influence of the hydrolysis duration and the enzyme concentration on the IC50 of the DPPH and ABTS [...] Read more.
The optimization of antioxidant and anti-tyrosinase activity during jellyfish hydrolysate preparation was studied using a response surface methodology (RSM) with a face-centered composite design. The influence of the hydrolysis duration and the enzyme concentration on the IC50 of the DPPH and ABTS radical scavenging activity, ferric-reducing antioxidant power (FRAP), the degree of hydrolysis (DH), yield, and the IC50 value of tyrosinase inhibitory activity were determined. The optimum conditions for the production of jellyfish hydrolysate using alcalase (JFAH), flavourzyme (JFFH), or papain (JFPH) were achieved at hydrolysis times of 360, 345, or 360 min, respectively, and at an enzyme concentration of 5.0%. JFFH had the highest antioxidant and tyrosinase inhibitory activity. JFAH, JFFH, and JFPH concentrations of 2.5 mg/mL resulted in HaCaT cells (IC80) having a survival rate of 80%. The amino acid profile of JFFH contained about 43% hydrophobic and 57% hydrophilic amino acids, comprising Gly, Cys, Glx, Asx, which were dominant. The isolation of a peptide fraction from JFFH was carried out using ultrafiltration membranes (10, 3, and 1 kDa) and gel filtration chromatography. Fraction-III (1–3 kDa) showed the highest antioxidative and tyrosinase inhibitory activity. Full article
(This article belongs to the Special Issue Food By-Products as a Source of Proteins and Peptides)
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14 pages, 3606 KiB  
Article
Multifunctionality of Rapeseed Meal Protein Isolates Prepared by Sequential Isoelectric Precipitation
by Radoslav Georgiev, Hristo Kalaydzhiev, Petya Ivanova, Cristina L. M. Silva and Vesela I. Chalova
Foods 2022, 11(4), 541; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11040541 - 14 Feb 2022
Cited by 3 | Viewed by 2248
Abstract
Rapeseed meal is a by-product of the oil-producing industry with a currently underestimated application. Two protein isolates, PI2.5–8.5 or PI10.5–2.5, were obtained from industrial rapeseed meal after treatment with an aqueous ethanol solution. The alkaline-extracted proteins were sequentially precipitated by [...] Read more.
Rapeseed meal is a by-product of the oil-producing industry with a currently underestimated application. Two protein isolates, PI2.5–8.5 or PI10.5–2.5, were obtained from industrial rapeseed meal after treatment with an aqueous ethanol solution. The alkaline-extracted proteins were sequentially precipitated by two different modes, from pH 10.5 to 2.5, and vice versa, from 2.5 to 8.5, with a step of 1 pH unit. The preparation approach influenced both the functional and antioxidant properties of the isolates. The PI10.5–2.5 exhibited higher water and oil absorption capacities than PI2.5–8.5, reaching 2.68 g H2O/g sample and 2.36 g oil/g sample, respectively. The emulsion stability of the PI2.5–8.5, evaluated after heating at 80 °C, was either 100% or close to 100% for all pH values studied (from 2 to 10), except for pH 6 where it reached 93.87%. For the PI10.5–2.5, decreases in the emulsion stability were observed at pH 8 (85.71%) and pH 10 (53.15%). In the entire concentration range, the PI10.5–2.5 exhibited a higher scavenging ability on 2,2-diphenyl-1-picryl hydrazyl (DPPH) and hydroxyl radicals than PI2.5–8.5 as evaluated by DPPH and 2-deoxyribose assays, respectively. At the highest concentration studied, 1.0%, the neutralization of DPPH radicals by PI10.5–2 reached half of that exhibited by synthetic antioxidant butylhydroxytoluene (82.65%). At the same concentration, the inhibition of hydroxyl radicals by PI10.5–2 (71.25%) was close to that achieved by mannitol (75.62%), which was used as a positive control. Established antioxidant capacities add value to the protein isolates that can thus be used as both emulsifiers and antioxidants. Full article
(This article belongs to the Special Issue Food By-Products as a Source of Proteins and Peptides)
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18 pages, 4520 KiB  
Article
Purification and Characterization of a Novel Calcium-Binding Heptapeptide from the Hydrolysate of Tilapia Bone with Its Osteogenic Activity
by Jinlun He, Hao Guo, Mei Zhang, Meng Wang, Liping Sun and Yongliang Zhuang
Foods 2022, 11(3), 468; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11030468 - 04 Feb 2022
Cited by 18 | Viewed by 2771
Abstract
In this study, a calcium-binding peptide was obtained by hydrolyzing tilapia bone and its osteogenic activity was evaluated. Animal protease was selected from nine enzymes, and its hydrolysate was purified through preparative and semi-preparative reverse phase high-performance liquid chromatography. The purified peptide was [...] Read more.
In this study, a calcium-binding peptide was obtained by hydrolyzing tilapia bone and its osteogenic activity was evaluated. Animal protease was selected from nine enzymes, and its hydrolysate was purified through preparative and semi-preparative reverse phase high-performance liquid chromatography. The purified peptide was identified as DGPSGPK (656.32 Da) and its calcium-binding capacity reached 111.98 µg/mg. The peptide calcium chelate (DGPSGPK-Ca) was obtained, and its structure was characterized through Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM), and mass spectrometry (MS). The results of XRD and SEM showed that DGPSGPK-Ca was formed as a new compound. The carboxyl and amino groups of Lys and Asp residues may be the chelating sites of DGPSGPK according to the FTIR and MS results. The molecular simulation showed the carbonyl groups of Asp, Pro, Ser, and Lys residues involved in the binding of calcium. The interaction of DGPSGPK and different integrins was evaluated by molecular docking simulation, and the main forces involved were electrostatic interaction forces, hydrogen bonding and hydrophobic interactions. Furthermore, DGPSGPK could inhibit the differentiation of osteoclast and promote the proliferation, differentiation and mineralization of osteoblasts. Full article
(This article belongs to the Special Issue Food By-Products as a Source of Proteins and Peptides)
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11 pages, 263 KiB  
Article
In Vitro Protein Digestibility of Selected Seaweeds
by Goldy De Bhowmick and Maria Hayes
Foods 2022, 11(3), 289; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11030289 - 21 Jan 2022
Cited by 20 | Viewed by 4588
Abstract
Seaweed biomass is considered a valuable and potential, alternative protein source but it is currently under-exploited. Seaweed or Macroalgae do not require arable land and freshwater for their cultivation, they are fast growing and contain several health ingredients and beneficial macronutrients. In this [...] Read more.
Seaweed biomass is considered a valuable and potential, alternative protein source but it is currently under-exploited. Seaweed or Macroalgae do not require arable land and freshwater for their cultivation, they are fast growing and contain several health ingredients and beneficial macronutrients. In this study, we determined the in vitro k-Protein Digestibility-Corrected Amino Acid Score (k-PDCAAS) values of six different, Irish seaweeds using the rapid k-PDCAAS method. Based on the amino acid profile and protein content of each seaweed, the in vitro protein digestibility and k-PDCAAS scores were calculated. In addition, the limiting amino acid(s) for each of the six seaweeds was/were determined. Results suggest that although the in vitro digestibility was quite similar for all analyzed seaweeds, their k-PDCAAS scores varied significantly. The red seaweed Palmaria palmata had a k-PDCAAS score of 0.69 ± 0.014, while Fucus serratus had a value of 0.63 ± 0.084 and Alaria esculenta a value of 0.59 ± 0.021. The seaweeds were found to be rich in essential amino acids and taurine. Overall, the amino acid composition of the seaweeds studied suggests that they are suitable alternative protein sources for use in human nutrition providing both essential and non-essential amino acids to the consumer. Full article
(This article belongs to the Special Issue Food By-Products as a Source of Proteins and Peptides)
22 pages, 1894 KiB  
Article
Quality of Protein Isolates and Hydrolysates from Baltic Herring (Clupea harengus membras) and Roach (Rutilus rutilus) Produced by pH-Shift Processes and Enzymatic Hydrolysis
by Tanja Kakko, Annelie Damerau, Anni Nisov, Anna Puganen, Saska Tuomasjukka, Kaisu Honkapää, Marko Tarvainen and Baoru Yang
Foods 2022, 11(2), 230; https://0-doi-org.brum.beds.ac.uk/10.3390/foods11020230 - 15 Jan 2022
Cited by 13 | Viewed by 3651
Abstract
Fractionation is a potential way to valorize under-utilized fishes, but the quality of the resulting fractions is crucial in terms of their applicability. The aim of this work was to study the quality of protein isolates and hydrolysates extracted from roach (Rutilus [...] Read more.
Fractionation is a potential way to valorize under-utilized fishes, but the quality of the resulting fractions is crucial in terms of their applicability. The aim of this work was to study the quality of protein isolates and hydrolysates extracted from roach (Rutilus rutilus) and Baltic herring (Clupea harengus membras) using either pH shift or enzymatic hydrolysis. The amino acid composition of protein isolates and hydrolysates mostly complied with the nutritional requirements for adults, but protein isolates produced using pH shift showed higher essential to non-essential amino acid ratios compared with enzymatically produced hydrolysates, 0.84–0.85 vs. 0.65–0.70, respectively. Enzymatically produced protein hydrolysates had a lower total lipid content, lower proportion of phospholipids, and exhibited lower degrees of protein and lipid oxidation compared with pH-shift-produced isolates. These findings suggest enzymatic hydrolysis to be more promising from a lipid oxidation perspective while the pH-shift method ranked higher from a nutrient perspective. However, due to the different applications of protein isolates and hydrolysates produced using pH shift or enzymatic hydrolysis, respectively, the further optimization of both studied methods is recommended. Full article
(This article belongs to the Special Issue Food By-Products as a Source of Proteins and Peptides)
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