Increased solubility and functional properties of precipitated Alfalfa protein concentrate subjected to pH shift processes

Nissen, Signe Hjerrild; Schmidt, Jesper Malling; Gregersen, Sandra Beyer; Hammershøj, Marianne; Møller, Anders Hauer; Danielsen, Marianne; Stødkilde, Lene; Nebel, Caroline; Dalsgaard, Trine Kastrup

doi:10.1016/j.foodhyd.2021.106874

Cited by 54 publications

(24 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In a continuation hereof, solutions of both 7% soluble alfalfa leaf protein and 13% whey protein isolate at pH 7 form standing gels; however, the alfalfa protein forms forms fine-stranded clear gels . The gel strength of alfalfa protein gels increased when subjecting the protein concentrate to a pH-shift solubilization …”

Section: Functionalityleaf Protein In Food Applicationsmentioning

confidence: 92%

“…53 The gel strength of alfalfa protein gels increased when subjecting the protein concentrate to a pH-shift solubilization. 172 At 2.5−10% protein concentration and salt levels of 0−0.2 M NaCl, spinach RuBisCo gels at a lower onset temperature compared with gels of whey protein and egg white protein. 83 Furthermore, the spinach protein gel has higher storage modulus (G′) and gel strength in texture analysis at comparable protein concentrations.…”

Section: Solubility Of Proteinsmentioning

confidence: 97%

“…However, at pH near the pI (i.e., pH 3−4.5), electrostatic repulsion is low and allows for proteins to interact at the air−water interface and facilitates the buildup of a stabilizing protein film. Nissen et al (2021) 172 found that the foam overrun and foam stability can be improved through the use of a pH-shift method, as well as addition of salt. Protein concentration increases the foam capacity up to a critical concentration, where a saturation level or steady state condition is reached.…”

Section: Solubility Of Proteinsmentioning

confidence: 99%

“…The minimum solubility is observed at pH 3.5–5 (∼10% soluble), which correlates to RuBisCo having a isoelectric point around pH 4.5 . The solubility is slightly higher at pH 2 and increases from pH 5 to a maximum of ∼80% at pH 10. ,,,, Using a pH-shift method where the protein concentrate is solubilized at pH 11 or 12 prior to readjustment to pH 7 increases the protein solubility at pH 7, but the alkaline pH also induce formation of protein cross-linking products, lanthionine, and lysinoalanine, which lowers the content of the essential amino acids, cysteine, and lysine and lowers the protein digestibility and may as well change other functional properties. Similarly, the solubility of leaf protein from perennial ryegrass was improved by solubilizing at alkaline pH before readjusting to neutral pH …”

Section: Functionalityleaf Protein In Food Applicationsmentioning

confidence: 99%

See 3 more Smart Citations

Biorefinery of Green Biomass─How to Extract and Evaluate High Quality Leaf Protein for Food?

Møller

Hammershøj

Passos

et al. 2021

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

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. Despite this, very little RuBisCo is utilized for foods because proteins in the leaf material has a low accessibility to monogastrics. In order to utilize the leaf protein for food purposes, the protein needs to be extracted from the fiber rich leaf matrix. This conversion of green biomass to valuable products has been labeled green biorefinery. The green biorefinery may be tailored to produce different products, but in this Review, the focus is on production of food-grade protein. The existing knowledge on the extraction, purification, and concentration of protein from green biomass is reviewed. Additionally, the quality and potential application of the leaf protein in food products and side streams from the green biorefinery will be discussed along with possible uses of side streams from the protein production.

show abstract

Section: Functionalityleaf Protein In Food Applicationsmentioning

confidence: 92%

Section: Solubility Of Proteinsmentioning

confidence: 97%

Section: Solubility Of Proteinsmentioning

confidence: 99%

Section: Functionalityleaf Protein In Food Applicationsmentioning

confidence: 99%

See 2 more Smart Citations

Biorefinery of Green Biomass─How to Extract and Evaluate High Quality Leaf Protein for Food?

Møller

Hammershøj

Passos

et al. 2021

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

show abstract

“…The maximum solubility (100%) of these proteins was obviously found at a pH of ~8.0 for both the Thai and Peru SI samples. The maximum solubility could be due to more hydrophilic linkages of the protein molecules with lower hydrophobicity to achieve higher solubility [29]. On the other hand, the Thai SI sample has the lowest solubility value and aggregation occurs at a pH of 4.5 to 5.…”

Section: Solubilitymentioning

confidence: 99%

Physicochemical, Functional, and In Vitro Digestibility of Protein Isolates from Thai and Peru Sacha Inchi (Plukenetia volubilis L.) Oil Press-Cakes

Rawdkuen

D’Amico

Schoenlechner

2022

Foods

View full text Add to dashboard Cite

Proteins from Sacha inchi (SI) have been widely known for their health-benefiting properties. This study aimed to investigate the different protein isolates obtained from oil press-cakes of Thai and Peru SI. The protein content and protein recovery of Thai and Peru SI were estimated to be 93.27, 90.67%, and 49.15, 59.32%, respectively. The protein patterns of the Thai and Peru SI samples analyzed by SDS-PAGE showed glycoprotein as a major protein, with a molecular weight of 35 kDa. Both protein isolates (PI) showed water and oil holding capacities in the range of 2.97–3.09 g/g sample and 2.75–2.88 g/g sample, respectively. The emulsifying properties of the PI from Thai SI were higher than those of Peru (p < 0.05), while the foaming properties were not analogous to the emulsion properties. The Thai SI sample showed lower digestibility up to 120 min of in vitro digestion time than that of the Peru SI sample (p < 0.05). However, simulated in vitro pepsin digestion of Thai and Peru Si samples displayed hydrolyzed protein bands compared to trypsin digestion, which showed no protein patterns in both SI samples on a 4–20% gradient gel. These results suggest that the protein isolates from Thai and Peru SI exhibit marked variations in physical and techno-functional properties and have a high potential to be employed as plant-based protein additives for future non-animal-based protein-rich foods.

show abstract

Pork liver as a source of protein with excellent foaming properties

Feliu-Alsina,

Saguer

2023

Eur Food Res Technol

View full text Add to dashboard Cite

Pork liver is a protein-rich offal, generated in large quantities in the meat industry and considered non-allergenic, although not highly appreciated by Western consumers. The recovery of its proteins through a simple and easily scalable process with the purpose of obtaining economical and environmentally friendly techno-functional ingredients might be an alternative for its valorization. Of great interest are protein fractions with good foaming properties that can act as substitutes for other highly allergenic proteins in food formulation. In this study, protein extractions from fresh pork livers were performed using buffer solutions adjusted to different pH (from 4.0 to 8.5), without a subsequent concentration/purification step. The main parameters evaluated were yield and foaming properties of the recovered extracts; their physicochemical characteristics and the SDS-PAGE protein profiles were determined as well. Acceptable extraction yields (> 50% of the total protein) were obtained using buffer solutions adjusted to pH ≥ 4.80, but their foaming properties were poor. By contrast, the extracts recovered using buffers adjusted to pH ≤ 4.75 were capable of forming very voluminous and stable foams, although rather low yields were achieved under these conditions (31.5–36.0% of the total protein). In addition to the profile of solubilized proteins, a low fat and relatively high carbohydrate content in the extracts seem to contribute to their excellent foaming properties. Therefore, protein extracts from fresh pork liver obtained using buffer solutions adjusted to pH 4.0–4.5 (extract pH: 5.3–5.6) could be a real alternative to other protein foaming agents that cause food allergies, in a simple, cost-effective and sustainable way.

show abstract

Increased solubility and functional properties of precipitated Alfalfa protein concentrate subjected to pH shift processes

Cited by 54 publications

References 36 publications

Biorefinery of Green Biomass─How to Extract and Evaluate High Quality Leaf Protein for Food?

Biorefinery of Green Biomass─How to Extract and Evaluate High Quality Leaf Protein for Food?

Physicochemical, Functional, and In Vitro Digestibility of Protein Isolates from Thai and Peru Sacha Inchi (Plukenetia volubilis L.) Oil Press-Cakes

Pork liver as a source of protein with excellent foaming properties

Contact Info

Product

Resources

About