Comparative study of gelation and cross-link formation during enzymatic texturisation of leguminous proteins

Schäfer, Christian; Zacherl, Christian; Engel, Karl‐Heinz; Neidhart, Sybille; Carle, Reinhold

doi:10.1016/j.ifset.2007.01.005

Cited by 20 publications

(8 citation statements)

References 38 publications

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“…1 Although most studies have been directed at meat, seafood and dairy proteins, the influence of MTG crosslinking on some technical and physiological functionalities of soy and other plant proteins has already been reported. 2–5…”

Section: Introductionmentioning

confidence: 99%

“…1 Although most studies have been directed at meat, seafood and dairy proteins, the inuence of MTG crosslinking on some technical and physiological functionalities of soy and other plant proteins has already been reported. [2][3][4][5] The extent of the crosslinking reaction is dependent on environmental conditions (pH, temperature, and the absence of enzyme inhibitors) and the structure and conformation of the target protein(s). Several studies have shown that non-globular proteins are more easily accessible to MTG crosslinking activity than globular proteins.…”

Section: Introductionmentioning

confidence: 99%

“…6,7 Also, different vegetable proteins have shown different susceptibilities to the MTG crosslinking activity. 4 Therefore, despite the ease of MTG in crosslinking various proteins, many of them, particularly globular proteins, are not affected by MTG in their native state due to the inaccessibility of the reactive residues buried within the protein tertiary structure.…”

Section: Introductionmentioning

confidence: 99%

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Effects of high-pressure and transglutaminase, individually and simultaneously applied, on pea and soy protein isolates

Neto Queirós,

Cruz Pinto,

Lopes-da-Silva

et al. 2023

Sustainable Food Technol.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Effects of high-pressure and transglutaminase, individually and simultaneously applied, on pea and soy protein isolates

Neto Queirós,

Cruz Pinto,

Lopes-da-Silva

et al. 2023

Sustainable Food Technol.

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show abstract

“…To improve the techno-functional properties, the addition of some gelation coadjuvant such as microbial transglutaminase would be very convenient in combination with different concentration of pea protein isolate. (Schäfer et al, 2007(Schäfer et al, , 2011Shand et al, 2008). However, the initial pea protein denaturation of commercial PPI could make it difficult the protein gelation by the formation of protein polymers linked by inter-and intra-molecular cross-links and the formation of new disulphide bonds between adjacent proteins (Marco et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Gelation of commercial pea protein isolate: effect of microbial transglutaminase and thermal processing

et al. 2020

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In the studied commercial pea protein isolate (PPI) some physicochemical modifications are induced in the protein structure during its processing. That fact would result into a reduction of proteins techno-functional properties. It has been evidenced by Differential Scanning Calorimetry the protein denaturation what gives as a result poor gelling ability. Microbial transglutaminase (MTGase) was added at different concentrations to improve the gelation process at two different settings/thermal treatments to make suitable texture PPI gels as a base for various meat and/or seafood analogues. SDS-PAGE analysis indicated that MTGase activity was focused on the polymerization of vicilins and legumins resulting in the promotion of new intermolecular protein complexes (increase in β-sheet aggregates). Rheological data showed that at 23% PPI with 5 and 7 U/g protein of MTGase the gel strength increased in terms of breaking force and complex modulus. It also improved the conformational stability and flexibility of their gel networks. The results suggest that appropriate gels with 23% PPI could be obtained adding 5 U/g MTGase able to be used as meat and/or seafood analogues.

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“…TG is predominantly used to alter the functionality of proteins of animal origin and has a wide application in the dairy industry and meat and fi sh processing (18). However, successful application of TG to alter plant protein functionality for the production of tofu, bread and other wheat products has also been reported (19,20).…”

Section: Introductionmentioning

confidence: 99%

Pepsin-Assisted Transglutaminase Modification of Functional Properties of a Protein Isolate Obtained from Industrial Sunflower Meal

Ivanova

Chalova

Kalaydzhiev

et al. 2017

Food Technol. Biotechnol.

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The utilization of industrial sunflower meal to produce protein-rich products for the food industry is an alternative approach for better and more efficient use of this agricultural by-product. Sunflower meal proteins possess specific functional properties, which however need improvement to broaden their potential as supplements for delivering high--quality products for human nutrition. The aim of the study is to evaluate the combined influence of low-degree pepsin hydrolysis and transglutaminase (TG) modification on industrial sunflower meal protein isolate functionality at pH=2 to 10. Three TG-modified pepsin hydrolysates with the degree of hydrolysis of 0.48, 0.71 and 1.72% were produced and named TG-PH1, TG-PH2 and TG-PH3, respectively. All three TG-modified pepsin hydrolysates exhibited improved solubility at pH between 3.5 and 5.5 as the highest was observed of TG-PH3 at protein isoelectric point (pI=4.5). Sunflower meal protein isolate and TG-modified sunflower meal protein isolate had greater solubility than the three TG-modified hydrolysates at pH<3 and >7. Significant improvement of foam making capacity (p<0.05) was achieved with all three TG-modified pepsin hydrolysates in the entire pH area studied. Pepsin hydrolysis of the protein isolate with the three degrees of hydrolysis did not improve foam stability. Improved thermal stability was observed with TG-PH3 up to 80 °C compared to the protein isolate (pH=7). At 90 °C, TG modification of the protein isolate alone resulted in the highest thermal stability. Pepsin hydrolysis followed by a treatment with TG could be used to produce sunflower protein isolates with improved solubility, foam making capacity and thermal stability for use in the food industry.

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Comparative study of gelation and cross-link formation during enzymatic texturisation of leguminous proteins

Cited by 20 publications

References 38 publications

Effects of high-pressure and transglutaminase, individually and simultaneously applied, on pea and soy protein isolates

Effects of high-pressure and transglutaminase, individually and simultaneously applied, on pea and soy protein isolates

Gelation of commercial pea protein isolate: effect of microbial transglutaminase and thermal processing

Pepsin-Assisted Transglutaminase Modification of Functional Properties of a Protein Isolate Obtained from Industrial Sunflower Meal

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