Textured Wheat and Pea Proteins for Meat Alternative Applications

Insertion of plastidic β-barrel proteins into the outer envelopes of plastids involves an intermembrane space intermediate formed with Toc75-V/OEP80

The Plant Cell ◽

10.1093/plcell/koab052 ◽

2021 ◽

Author(s):

Lucia E Gross ◽

Anna Klinger ◽

Nicole Spies ◽

Theresa Ernst ◽

Nadine Flinner ◽

...

Keyword(s):

Membrane Proteins ◽

Protein Import ◽

Membrane Insertion ◽

Intermembrane Space ◽

Envelope Membrane ◽

Outer Envelope ◽

Pea Proteins ◽

Outer Envelope Membrane ◽

Correct Topology ◽

Shed Light

Abstract The insertion of organellar membrane proteins with the correct topology requires the following: First, the proteins must contain topogenic signals for translocation across and insertion into the membrane. Second, proteinaceous complexes in the cytoplasm, membrane, and lumen of organelles are required to drive this process. Many complexes required for the intracellular distribution of membrane proteins have been described, but the signals and components required for the insertion of plastidic β-barrel-type proteins into the outer membrane are largely unknown. The discovery of common principles is difficult, as only a few plastidic β-barrel proteins exist. Here, we provide evidence that the plastidic outer envelope β-barrel proteins OEP21, OEP24, and OEP37 from pea (Pisum sativum) and Arabidopsis thaliana contain information defining the topology of the protein. The information required for translocation of pea proteins across the outer envelope membrane is present within the six N-terminal β-strands. This process requires the action of TOC (translocon of the outer chloroplast membrane). After translocation into the intermembrane space, β-barrel proteins interact with TOC75-V, as exemplified by OEP37 and P39, and are integrated into the membrane. The membrane insertion of plastidic β-barrel proteins is affected by mutation of the last β-strand, suggesting that this strand contributes to the insertion signal. These findings shed light on the elements and complexes involved in plastidic β-barrel protein import.

Pea proteins: variation, composition, genetics, and functional properties

Cereal Chemistry ◽

10.1002/cche.10439 ◽

2021 ◽

Author(s):

Sintayehu D. Daba ◽

Craig F. Morris

Keyword(s):

Functional Properties ◽

Pea Proteins

Interaction of selected volatile flavour compounds and salt-extracted pea proteins: Effect on protein structure and thermal-induced gelation properties

Food Hydrocolloids ◽

10.1016/j.foodhyd.2015.05.044 ◽

2015 ◽

Vol 51 ◽

pp. 383-394 ◽

Cited By ~ 5

Author(s):

Kun Wang ◽

Susan D. Arntfield

Keyword(s):

Protein Structure ◽

Flavour Compounds ◽

Pea Proteins ◽

Volatile Flavour

Effect of salts and pH on selected ketone flavours binding to salt-extracted pea proteins: The role of non-covalent forces

Food Research International ◽

10.1016/j.foodres.2015.03.017 ◽

2015 ◽

Vol 77 ◽

pp. 1-9 ◽

Cited By ~ 12

Author(s):

Kun Wang ◽

Susan D. Arntfield

Keyword(s):

Pea Proteins

Rheological and microstructural characterization of batters and sponge cakes fortified with pea proteins

Food Hydrocolloids ◽

10.1016/j.foodhyd.2019.105553 ◽

2020 ◽

Vol 101 ◽

pp. 105553 ◽

Cited By ~ 3

Author(s):

M. Assad Bustillos ◽

C. Jonchère ◽

C. Garnier ◽

A.L. Réguerre ◽

G. Della Valle

Keyword(s):

Microstructural Characterization ◽

Pea Proteins

Preheat-stabilized pea proteins with anti-aggregation properties

International Journal of Biological Macromolecules ◽

10.1016/j.ijbiomac.2019.11.100 ◽

2020 ◽

Vol 155 ◽

pp. 1288-1295

Author(s):

Chao Wu ◽

Jiamei Wang ◽

Wuchao Ma ◽

Yiru Cai ◽

Tao Wang

Keyword(s):

Pea Proteins

Synergistic enhancement in the co-gelation of salt-soluble pea proteins and whey proteins

Food Chemistry ◽

10.1016/j.foodchem.2013.05.082 ◽

2013 ◽

Vol 141 (4) ◽

pp. 3913-3919 ◽

Cited By ~ 18

Author(s):

Douglas Wong ◽

Thava Vasanthan ◽

Lech Ozimek

Keyword(s):

Whey Proteins ◽

Synergistic Enhancement ◽

Pea Proteins

Are Faba Bean and Pea Proteins Potential Whey Protein Substitutes in Infant Formulas? An In Vitro Dynamic Digestion Approach

Foods ◽

10.3390/foods9030362 ◽

2020 ◽

Vol 9 (3) ◽

pp. 362

Author(s):

Linda Le Roux ◽

Olivia Ménard ◽

Raphaël Chacon ◽

Didier Dupont ◽

Romain Jeantet ◽

...

Keyword(s):

Faba Bean ◽

Whey Proteins ◽

Milk Proteins ◽

Protein Digestibility ◽

Cow Milk ◽

Partial Substitution ◽

Infant Formulas ◽

Pea Proteins

Infant formulas (IFs) are used as substitutes for human milk and are mostly based on cow milk proteins. For sustainability reasons, animal protein alternatives in food are increasingly being considered, as plant proteins offer interesting nutritional and functional benefits for the development of innovative IFs. This study aimed to assess how a partial substitution (50%) of dairy proteins with faba bean and pea proteins influenced the digestibility of IFs under simulated dynamic in vitro digestion, which were set up to mimic infant digestion. Pea- and faba bean-based IFs (PIF and FIF, respectively) have led to a faster aggregation than the reference milk-based IF (RIF) in the gastric compartment; that did not affect the digesta microstructure at the end of digestion. The extent of proteolysis was estimated via the hydrolysis degree, which was the highest for FIF (73%) and the lowest for RIF (50%). Finally, it was apparent that in vitro protein digestibility and protein digestibility-corrected amino acid score (PDCAAS)-like scores were similar for RIF and FIF (90% digestibility; 75% PDCAAS), but lower for PIF (75%; 67%). Therefore, this study confirms that faba bean proteins could be a good candidate for partial substitution of whey proteins in IFs from a nutritional point of view, provided that these in vitro results are confirmed in vivo.

Utilization of plant-based protein-polyphenol complexes to form and stabilize emulsions: Pea proteins and grape seed proanthocyanidins

Food Chemistry ◽

10.1016/j.foodchem.2020.127219 ◽

2020 ◽

Vol 329 ◽

pp. 127219

Author(s):

Taotao Dai ◽

Ti Li ◽

Ruyi Li ◽

Hualu Zhou ◽

Chengmei Liu ◽

...

Keyword(s):

Grape Seed ◽

Grape Seed Proanthocyanidins ◽

Pea Proteins

Amino Acid Availability of a Dairy and Vegetable Protein Blend Compared to Single Casein, Whey, Soy, and Pea Proteins: A Double-Blind, Cross-Over Trial

Nutrients ◽

10.3390/nu11112613 ◽

2019 ◽

Vol 11 (11) ◽

pp. 2613 ◽

Cited By ~ 5

Author(s):

Jue Liu ◽

Marianne Klebach ◽

Monique Visser ◽

Zandrie Hofman

Keyword(s):

Amino Acid ◽

Protein Quality ◽

Tube Feeding ◽

Area Under The Curve ◽

Amino Acid Profile ◽

Elderly Subjects ◽

Double Blind ◽

Healthy Elderly ◽

Amino Acid Availability ◽

Pea Proteins

Protein quality is important for patients needing medical nutrition, especially those dependent on tube feeding. A blend of dairy and vegetable proteins (35% whey, 25% casein, 20% soy, 20% pea; P4) developed to obtain a more balanced amino acid profile with higher chemical scores, was compared to its constituent single proteins. Fourteen healthy elderly subjects received P4, whey, casein, soy, and pea (18 g/360 mL bolus) on five separate visits. Blood samples were collected at baseline until 240 min after intake. Amino acid availability was calculated using incremental maximal concentration (iCmax) and area under the curve (iAUC). Availability for P4 as a sum of all amino acids was similar to casein (iCmax and iAUC) and whey (iCmax) and higher vs. soy (iCmax and iAUC) and pea (iCmax). Individual amino acid availability (iCmax and iAUC) showed different profiles reflecting the composition of the protein sources: availability of leucine and methionine was higher for P4 vs. soy and pea; availability of arginine was higher for P4 vs. casein and whey. Conclusions: The P4 amino acid profile was reflected in post-prandial plasma levels and may be regarded as more balanced compared to the constituent single proteins.