Formation of heat-induced cottonseed congossypin(7S) fibrils at pH 2.0

Zhou, Jing; Zhang, Hui; Hong-yuan, Yang; Wang, Li; Qian, Haifeng

doi:10.1002/jsfa.6517

Cited by 15 publications

(7 citation statements)

References 28 publications

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“…Our results show that GCSM has major protein bands between 13,273 and 56,564 Da, which are adequate for protein texturization (Jafari, Rajabzadeh, Tabtabaei, Marsolais, & Legge, ). Other authors (Sun et al., ; Zhou, Zhang, Yang, Wang, & Qian, ), also found two protein dimmers with a molecular weight between 43,000 and 97,400 Da in cottonseed proteins similar to our protein patterns, after protein extraction with NaCl solution. The salt‐soluble proteins from GCSM have a similar electrophoretic (SDS‐PAGE) pattern to water‐soluble proteins present in soybean and similar protein yields with salt and alkaline extraction (Gorinstein et al., ; Muranyi et al., ).…”

Section: Resultssupporting

confidence: 89%

Characterization of Soluble Glandless Cottonseed Meal Proteins Based on Electrophoresis, Functional Properties, and Microscopic Structure

Delgado

Valverde-Quiroz

Lopez

et al. 2019

Journal of Food Science

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This investigation aimed to extract and characterize the GCSM proteins, determine their solubility potential at two different temperatures and different solvents, and explore their functional properties. During the extraction, no water‐ or ethanol‐soluble protein was found. Most of the protein was extracted with KOH solution. GCSM showed major protein bands between 13,273 and 56,564 Da with an isoelectric point of 5.1. The results showed that extraction temperature and solvent affected the amount of protein extracted from GCSM. The highest protein yield (63.4%) was obtained with KOH at 55 °C. Fat content negatively affected the protein solubility. The highest protein purity (99.9%) was obtained with 6% of fat content and the lowest one with 19% of fat content. GCSM has a high glutamic acid content, followed by arginine and aspartic acid compared to the other amino acids. The essential amino acids make up about 30.0% of the total amino acid concentration in KOH‐soluble fractions. The results showed a denaturation temperature of GCSM protein ranging from 61.4 to 63.6 °C. Scanning electron microscopy reveals a microglobular protein structure. GCSM protein isolate showed lower (P < 0.05) water‐holding and oil‐holding capacity but similar gelation properties as soy protein. GCSM protein shows a high foaming capacity at high pH values and high emulsion stability. Practical Application The results of this investigation have a direct impact on the plant protein processing industry. This paper presents a new source of plant protein with a high foaming capacity in alkaline conditions with potential applications for human consumption and feed for aquaculture and animals. The results of this research may impact the cotton producers who can increase their income, and the aquaculture industry will have a cheaper source of protein that can partially substitute the expensive fishmeal. Cottonseed protein can be used to develop high protein extruded snacks and other functional foods, such as plant protein‐based food products.

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Section: Resultssupporting

confidence: 89%

Characterization of Soluble Glandless Cottonseed Meal Proteins Based on Electrophoresis, Functional Properties, and Microscopic Structure

Delgado

Valverde-Quiroz

Lopez

et al. 2019

Journal of Food Science

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“… 8,9 Formation of PNFs at low pH and elevated temperature seem to be generic for many proteins of different sources, including e.g. soy protein, 10,11 green pea protein, 12 kidney bean phaseolin, 13 cottonseed congossypin, 14 and bovine caseins. 15 …”

Section: Introductionmentioning

confidence: 99%

“…soy protein, 10,11 green pea protein, 12 kidney bean phaseolin, 13 cottonseed congossypin, 14 and bovine caseins.…”

Section: 9mentioning

confidence: 99%

On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology

Hedenqvist

Langton

et al. 2018

RSC Adv.

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Self-assembly of proteins into amyloid-like nanofibrils is not only a key event in several diseases, but such fibrils are also associated with intriguing biological function and constitute promising components for new biobased materials. The bovine whey protein b-lactoglobulin has emerged as an important model protein for the development of such materials. We here report that peptide hydrolysis is the rate-determining step for fibrillation of b-lactoglobulin in whey protein isolate. We also explore the observation that blactoglobulin nanofibrils of distinct morphologies are obtained by simply changing the initial protein concentration. We find that the morphological switch is related to different nucleation mechanisms and that the two classes of nanofibrils are associated with variations of the peptide building blocks. Based on the results, we propose that the balance between protein concentration and the hydrolysis rate determines the structure of the formed nanofibrils.

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“…In order to achieve large-scale production of PNFs, it is desirable to move to proteins from large-scale resources. The finding over the last 10-15 years has presented several options (Table 3); for example, from cottonseed [33], soybean [26], cow milk [18,47], egg [25], and fish industry waste [23]. None of these proteins is connected to any function or malfunction but still form PNFs with similar structures as the classical amyloid proteins.…”

Section: Sourcesmentioning

confidence: 99%

“…Indeed, several different proteins have been reported to form nanofibrils when incubated at low pH (ca. 2) and high temperature (70°C-90°C) [24,26,28,33,47,60,61]. The generic fibrillation-promoting conditions is partly related to the uniform positive charge of the protein molecules at low pH, which direct the assembly process into ordered structures rather than disordered aggregates.…”

Section: Production Of Pnfsmentioning

confidence: 99%

Protein nanofibrils: Preparation, properties, and possible applications in industrial nanomaterials

Lendel

Langton

et al. 2019

Industrial Applications of Nanomaterials

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Formation of heat-induced cottonseed congossypin(7S) fibrils at pH 2.0

Abstract: The results would be of vital importance for the utilisation of cottonseed proteins to produce thermally induced fibrillar gels with excellent properties.

Cited by 15 publications

References 28 publications

Characterization of Soluble Glandless Cottonseed Meal Proteins Based on Electrophoresis, Functional Properties, and Microscopic Structure

Characterization of Soluble Glandless Cottonseed Meal Proteins Based on Electrophoresis, Functional Properties, and Microscopic Structure

On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology

Protein nanofibrils: Preparation, properties, and possible applications in industrial nanomaterials

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