Proteins from pseudocereal seeds: solubility, extraction, and modifications of the physicochemical and techno‐functional properties

Constantino, Augusto Bene Tomé; Garcia‐Rojas, Edwin Elard

doi:10.1002/jsfa.11750

Cited by 21 publications

(6 citation statements)

References 78 publications

(189 reference statements)

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“…One hundred grams of the powder were added to 1000 mL of 75% ethanol aqueous solution and mixed with a magnetic stirrer for 5 min [ 29 , 30 ]. Then, the samples were incubated for 120 min at 40 °C in a water bath (HH-S6, Oulaibo, Jinan, China).…”

Section: Methodsmentioning

confidence: 99%

The Composition, Structure, and Functionalities of Prolamins from Highland Barley

Xing

Zhang

et al. 2023

Molecules

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The composition, structure, and functionalities of prolamins from highland barley were investigated. These parameters were compared with those of the commonly applied prolamins (zein). There are more charged and hydrophilic amino acids in highland barely prolamins than zein. The molecular weight of highland barely prolamins was between 30 and 63 kDa, which was larger than that of zein (20 and 24 kDa). The main secondary structure of highland barely prolamins was β-turn helices, while α-helical structures were the main secondary structure in zein. The water holding capacity, thermal stability, emulsifying capacity, and stability of prolamins from highland barley were significantly higher than in zein, while the opposite results were observed for oil absorption capacity between the two. The diameter of fibers prepared using highland barely prolamins was almost six times that of zein, while highland barely prolamins formed ribbon structures instead of fibers. Therefore, the results provide guidance for applications of prolamins from highland barley.

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Section: Methodsmentioning

confidence: 99%

The Composition, Structure, and Functionalities of Prolamins from Highland Barley

Xing

Zhang

et al. 2023

Molecules

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“…The excellent solubility of protein allows them to be widely utilized in the food industry. 72 Initially, the solubility of MBP can be influenced by some intrinsic factors, such as its composition and structure. For example, the solubility of 11S globulins (20%) was higher than that of the 8S globulins (approximately 5%) at pH 4.0, but an opposite trend was observed when the pH was decreased to 2.0.…”

Section: Solubilitymentioning

confidence: 99%

“…The excellent solubility of protein allows them to be widely utilized in the food industry 72 . Initially, the solubility of MBP can be influenced by some intrinsic factors, such as its composition and structure.…”

Section: Functional Properties Of Mbpmentioning

confidence: 99%

Mung bean protein as an emerging source of plant protein: a review on production methods, functional properties, modifications and its potential applications

Feng,

Niu,

Zhang

et al. 2023

J Sci Food Agric

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Plant protein is rapidly becoming more of a prime interest to consumers for its nutritional and functional properties, as well as the potential to replace animal protein. In the frame of alternative protein new sources, mung bean is becoming another legume crop that could provide high quality plant protein after soybean and pea. In particular, the 8S globulins in mung bean protein have high structural similarity and homology with soybean β‐conglycinin (7S globulin), with 68% sequence identity. Currently, mung bean protein has gained popularity in food industry because of its high nutritional value and peculiar functional properties. In that regard, various modification technologies have been applied to further broaden its application. Here, we provide a review of the composition, nutritional value, production methods, functional properties and modification technologies of mung bean protein. Furthermore, its potential applications in the new plant‐based products, meat products, noodles, edible packaging films and bioactive compound carriers are highlighted to facilitate its utilization as an alternative plant protein, thus meeting consumer demands for high quality plant protein resources. © 2023 Society of Chemical Industry.

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“…The amino acids in quinoa are close to the amino acid composition mode recommended by the Food and Agriculture Organization of the United Nations. Moreover, quinoa has attracted extensive attention due to the lack of gluten protein, and thus quinoa is usually used as a food source for patients with celiac disease 2 . Gelation is one of the most important functional properties of many plant proteins.…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, quinoa has attracted extensive attention due to the lack of gluten protein, and thus quinoa is usually used as a food source for patients with celiac disease. 2 Gelation is one of the most important functional properties of many plant proteins. However, as the main raw material for gluten-free food, it is difficult for quinoa to build a superior crosslinked network structure because of the absence of gluten protein.…”

Section: Introductionmentioning

confidence: 99%

Synergistic improvement of quinoa protein heat‐induced gel properties treated by high‐intensity ultrasound combined with transglutaminase

Cao,

Wang,

Wang

et al. 2023

J Sci Food Agric

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BACKGROUNDQuinoa protein is enriched with a wide range of amino acids, including all nine essential amino acids necessary for the human body, and in appropriate proportions. However, as the main ingredient of gluten‐free food, it is difficult for quinoa to form a certain network structure for lack of gluten protein. The aim of this work was to enhance the gel properties of quinoa protein. Therefore, the texture characteristics of quinoa protein treated with different ultrasound intensities coupled with transglutaminase (TGase) were investigated.RESULTSThe gel strength of quinoa protein gel increased markedly by 94.12% with 600 W ultrasonic treatment, and the water holding capacity increased from 56.6% to 68.33%. The gel solubility was reduced and free amino content increased the apparent viscosity and the consistency index. Changes in the free sulfhydryl group and hydrophobicity indicated that ultrasound stretched protein molecules and exposed active sites. The enhanced intrinsic fluorescence intensity at 600 W demonstrated that ultrasonic treatment affected the conformation of quinoa protein. New bands emerged in sodium dodecylsulfate–polyacrylamide gel electrophoresis indicating that high‐molecular‐weight polymers were generated through TGase‐mediated isopeptide bonds. Furthermore, scanning electron microscopy showed that the gel network structure of TGase‐catalyzed quinoa protein was more uniform and denser, thereby improving the gel quality of quinoa protein.CONCLUSIONThe results suggested that high‐intensity ultrasound combined with TGase would be an effective way to develop higher‐quality quinoa protein gel. © 2023 Society of Chemical Industry.

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Proteins from pseudocereal seeds: solubility, extraction, and modifications of the physicochemical and techno‐functional properties

Cited by 21 publications

References 78 publications

The Composition, Structure, and Functionalities of Prolamins from Highland Barley

The Composition, Structure, and Functionalities of Prolamins from Highland Barley

Mung bean protein as an emerging source of plant protein: a review on production methods, functional properties, modifications and its potential applications

Synergistic improvement of quinoa protein heat‐induced gel properties treated by high‐intensity ultrasound combined with transglutaminase

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