Structure and functional properties of soy protein isolate-lentinan conjugates obtained in Maillard reaction by slit divergent ultrasonic assisted wet heating and the stability of oil-in-water emulsions

Wen, Chaoting; Zhang, Jixian; Wei, Qin; Gu, Jinyan; Zhang, Haihui; Duan, Yuqing; Ma, Haile

doi:10.1016/j.foodchem.2020.127374

Cited by 118 publications

(72 citation statements)

References 35 publications

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“…Changes in the secondary and tertiary structure of the protein, as well as their increased molecular weight, suggest that the conjugated carbohydrates on the emulsion-droplet surface provide steric stabilization against these environmental influences [120]. Similar observations were made for the foaming properties of glycated soy proteins [128][129][130]. Another emphasis of glycation studies on soy proteins is their allergenic potential.…”

Section: Glycation Of Major Plant Proteins 41 Grain Legumessupporting

confidence: 55%

“…It was shown that these additional treatments improve the functionality even further compared to conventional wet heating. Applying ultrasound treatment during wet heating increased the degree of glycation by 1.91 compared with traditional wet heating as well as the techno-functional performance of the glycated soy proteins [129]. Compared to emulsions stabilized by soy protein isolate and conventionally glycated soy protein isolate, the use of soy protein isolate that was glycated under the influence of irradiation led to lower creaming, oiling off, particle size, and flocculation degree after three freeze-thaw cycles of the emulsions [130].…”

Section: Glycation Of Major Plant Proteins 41 Grain Legumesmentioning

confidence: 98%

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Glycation of Plant Proteins Via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application

Kutzli

Weiß

Gibis

2021

Foods

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Plant proteins are being considered to become the most important protein source of the future, and to do so, they must be able to replace the animal-derived proteins currently in use as techno-functional food ingredients. This poses challenges because plant proteins are oftentimes storage proteins with a high molecular weight and low water solubility. One promising approach to overcome these limitations is the glycation of plant proteins. The covalent bonding between the proteins and different carbohydrates created via the initial stage of the Maillard reaction can improve the techno-functional characteristics of these proteins without the involvement of potentially toxic chemicals. However, compared to studies with animal-derived proteins, glycation studies on plant proteins are currently still underrepresented in literature. This review provides an overview of the existing studies on the glycation of the major groups of plant proteins with different carbohydrates using different preparation methods. Emphasis is put on the reaction conditions used for glycation as well as the modifications to physicochemical properties and techno-functionality. Different applications of these glycated plant proteins in emulsions, foams, films, and encapsulation systems are introduced. Another focus lies on the reaction chemistry of the Maillard reaction and ways to harness it for controlled glycation and to limit the formation of undesired advanced glycation products. Finally, challenges related to the controlled glycation of plant proteins to improve their properties are discussed.

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Section: Glycation Of Major Plant Proteins 41 Grain Legumessupporting

confidence: 55%

Section: Glycation Of Major Plant Proteins 41 Grain Legumesmentioning

confidence: 98%

Glycation of Plant Proteins Via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application

Kutzli

Weiß

Gibis

2021

Foods

View full text Add to dashboard Cite

show abstract

“…Changes in the secondary and tertiary structure of the protein as well as their increased molecular weight suggest that the conjugated carbohydrates on the emulsion droplet surface provide steric stabilization against these environmental influences [119]. Similar observations were made for the foaming properties of glycated soy proteins [127][128][129]. [205] RH: relative humidity PBS: phosphate-buffered saline…”

Section: Grain Legumesmentioning

confidence: 52%

“…It was shown that these additional treatments improve the functionality even further compared to conventional wet heating. Applying ultrasound treatment during wet heating increased the degree of glycation by 1.91 compared with traditional wet heating as well as the technofunctional performance of the glycated soy proteins [128]. Compared to emulsions stabilized by soy protein isolate and conventionally glycated soy protein isolate, the use of soy protein isolate which was glycated under the influence of irradiation led to lower creaming, oiling off, particle size, and flocculation degree after three freeze-thaw cycles of the emulsions [129].…”

Section: Grain Legumesmentioning

confidence: 98%

“…Wen et al [128] showed that glycation of soy protein isolate with lentinan by wet heating enhanced its foaming capacity and foam stability. This effect was even further promoted by using ultrasound-assisted wet heating since it enhanced the degree of glycation, which led to greater improvement of solubility, increase of the random structure of the protein as well as an increase of viscosity [128]. The foam stability of rice protein isolate could be increased by up to 2.74 times upon its glycation with dextran depending on the ratio of protein to polysaccharide used.…”

Section: Foamingmentioning

confidence: 99%

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Glycation of Plant Proteins via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application

Kutzli¹,

Weiß²,

Gibis³

2020

Preprint

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Plant proteins being considered to become the most important protein source of the future, they must be able to replace the animal-derived proteins currently in use as technofunctional food ingredients. This poses challenges because plant proteins are oftentimes storage proteins with a high molecular weight and low water solubility. One promising approach to overcome these limitations is the glycation of plant proteins. The covalent bonding between the proteins and different carbohydrates created via the initial stage of the Maillard reaction can improve the technofunctional characteristics of these proteins without the involvement of potentially toxic chemicals. However, compared to studies with animal-derived proteins, glycation studies on plant proteins are currently still underrepresented in literature. This review provides an overview of the existing studies on the glycation of the major groups of plant proteins with different carbohydrates using different preparation methods. Emphasis is put on the reaction conditions used for glycation as well as the modifications to physicochemical properties and technofunctionality. Different applications of these glycated plant proteins in emulsions, foams, films, and encapsulation systems are introduced. Another focus lies on the reaction chemistry of the Maillard reaction and ways to harness it for controlled glycation and to limit the formation of undesired advanced glycation products. Finally, challenges related to the controlled glycation of plant proteins to improve their properties are discussed.

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Effect of ultrasound pretreatment on the functional and antioxidant properties of fermented and germinated Lupin protein isolates grafted with glucose

İşçimen

Hayta

2021

J Sci Food Agric

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BACKGROUND This study examined the functional and antioxidant properties of Maillard reaction (MR) products of lupin protein isolate (LPI), fermented (FLPI), and germinated (GLPI) with glucose (G), treated with ultrasound (US) at different power levels (20–40–60–80%) for 15 min. The MR was conducted in a water bath for 180 min at 90 °C. RESULTS The Trolox‐equivalent antioxidant capacity (TEAC) values were found to be 46.79%, 56.43%, and 35.56% for the control (C), 58.99%, 80.17%, and 69.73% for conjugates of LPI‐G, FLPI‐G, and GLPI‐G treated at 80% US, respectively. The maximum 2,2‐diphenyl‐1‐picrylhydrazyl (DPPH) scavenging activity of LPI‐G, FLPI‐G, and GLPI‐G was found to be 39.68%, 59.54%, and 48.41%, respectively after 80% US. The FLPI‐G sample showed the highest antioxidant activity compared with the samples treated at the same power level for DPPH and TEAC. The Fe‐chelating activity of GLPI‐G showed significant differences when compared with FLPI‐G. The solubility of LPI‐G, FLPI‐G, and GLPI‐G increased with increasing US power. The highest solubility was 74.29% for 80% US‐treated GLPI‐G. The emulsifying activity index (EAI) increased at 20% US and decreased with further increase in the US power. The EAI and emulsifying stability index (ESI) were negatively affected by the MR and US processes. CONCLUSION The findings of current study proved that conjugation of LPI with G with the MR and with US pretreatment is an effective method for improving the bio‐ and techno‐functional properties of LPI. It is therefore likely that the properties of plant proteins modified by biochemical and physical treatments may widen their applications in the food industry. © 2021 Society of Chemical Industry.

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Structure and functional properties of soy protein isolate-lentinan conjugates obtained in Maillard reaction by slit divergent ultrasonic assisted wet heating and the stability of oil-in-water emulsions

Cited by 118 publications

References 35 publications

Glycation of Plant Proteins Via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application

Glycation of Plant Proteins Via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application

Glycation of Plant Proteins via Maillard Reaction: Reaction Chemistry, Technofunctional Properties, and Potential Food Application

Effect of ultrasound pretreatment on the functional and antioxidant properties of fermented and germinated Lupin protein isolates grafted with glucose

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