Enzymic modification of extruded soy protein concentrates as a method of obtaining new functional food components

Surówka, Krzysztof; Żmudziński, Daniel; Surówka, J.

doi:10.1016/j.tifs.2003.09.013

Cited by 55 publications

(45 citation statements)

References 26 publications

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“…This might be so because peptides released from a network structure of the sunflower protein reveal great flexibility, which helps them to adopt a conformation with hydrophilic groups more exposed outward. This kind of results was earlier observed for Alcalase-treated peanut protein isolate (Zhao et al 2011) and soybean protein concentrate (Surowka et al 2004).…”

Section: Resultssupporting

confidence: 84%

Modification of structural and functional properties of sunflower 11S globulin hydrolysates

Ren¹,

Song²,

Wang³

et al. 2015

Czech J. Food Sci.

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Ren J., Song Ch.-L., Wang P., Li S., Kopparapu N.-K., Zheng X.-Q. (2015): Modification of structural and functional properties of sunflower 11S globulin hydrolysates. Czech J. Food Sci., 33: 474-478.The structural and functional properties such as solubility, emulsifying properties, foaming properties, oil binding capacity, and surface hydrophobicity of sunflower 11S globulin hydrolysates generated by Alcalase at hydrolysis time of 30, 60, 90, and 120 min were evaluated. Circular dichroism analysis showed the hydrolysates possessed a decreased α-helix and β-structure. The hydrolysates exhibited lower surface hydrophobicity. Hydrolysates with shorter hydrolysis time showed the higher emulsifying activity index, but the same emulsion stability and oil binding capacity compared to the original 11S globulin. The longer hydrolysis resulted in lower foaming and emulsion stability. Thus it was demonstrated that by controlling the hydrolysis time of sunflower 11S globulin, hydrolysate with a desirable functional properties can be obtained.

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Section: Resultssupporting

confidence: 84%

Modification of structural and functional properties of sunflower 11S globulin hydrolysates

Ren¹,

Song²,

Wang³

et al. 2015

Czech J. Food Sci.

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show abstract

“…The case of limited hydrolysis is less conclusive. A decline in the surface hydrophobicity with limited hydrolysis has been reported for soybeans (Jung et al, 2005;Surowka, Zmudzinski, & Surowka, 2004), peanuts , and lentil proteins (Avramenko et al, 2013), in agreement with the present study. Jung et al (2005) proposed that the exposure of buried hydrophobic groups upon limited protein hydrolysis was followed by their aggregation via hydrophobic interactions, thus effectively reburying them within the interior of a larger aggregated structure, resulting in the reduction of surface hydrophobicity.…”

Section: Surface Hydrophobicitysupporting

confidence: 93%

Characterizing the structural and surface properties of proteins isolated before and after enzymatic demulsification of the aqueous extract emulsion of peanut seeds

Zhang

2015

Food Hydrocolloids

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“…Limited hydrolysis (4% DH) by both endo-and exopeptidase treatments significantly reduced the EC for enzyme hydrolysates compared with the control, with the exopeptidase hydrolysates showing the lowest EC values. This was in contrast to the generally recognized trend that EC increases with limited protein hydrolysis up to 5% DH (2,4,5,21). Extensive hydrolysis does have a detrimental effect on EC, but in our case, we observed decreased emulsification even at 4% DH.…”

Section: Resultscontrasting

confidence: 74%

“…This may partly explain the lack of a significant increase in emulsion stability for this enzyme hydrolysate. Short peptide chains would lead to decreased viscosity of the continuous phase and, although capable of adsorbing to the emulsion interfaces, they cannot form sufficiently strong barriers to prevent coalescence (2). Jet cooking the hydrolysates did not result in consistent trends in emulsion stability with regard to enzyme type.…”

Section: Resultsmentioning

confidence: 91%

Enzymatic hydrolysis of extruded‐expelled soy flour and resulting functional properties

Lamsal

Reitmeier

Murphy

et al. 2006

J Americ Oil Chem Soc

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Limited hydrolysis (4% degree of hydrolysis) of extruded-expelled soy flour protein (protein dispersibility index = 21) that was poor in solubility and other functional properties was evaluated at pilot-plant scale (5 kg of flour) with two endopeptidases and one exopeptidase. Some hydrolysates were merely spray-dried whereas others were jet-cooked at 104°C for 19 s before spray-drying. Solubility, emulsification capacity and stability, foaming capacity and stability, apparent viscosity, and sensory attributes were then characterized. The type of protease used and hydrothermal cooking affected functional and sensory properties. Protein solubility modestly increased with hydrolysis and jet cooking, but emulsification capacity decreased on hydrolysis and was not restored with hydrothermal cooking. Emulsion stability improved in the endopeptidase hydrolysates, but not in the exopeptidase hydrolysates. The foaming capacities of the hydrolysates for both types of enzymes were better than for the unhydrolyzed control. Highly stable foams were obtained after hydrolyzing with exopeptidase and hydrothermal cooking. Ten percent protein hydrolysate dispersions showed large losses in consistency coefficient and apparent viscosity, which increased significantly with hydrothermal cooking only for the unhydrolyzed control. Difference-from-control sensory evaluation indicated that both jet-cooked and non-jet-cooked enzyme hydrolysates were different from unhydrolyzed controls.Food proteins are critical components of foods owing to their important functional or physicochemical and nutritional contributions. Food protein ingredients are increasingly expected to perform functional roles that are critical to processing efficiency and consumer acceptance of foods. Functional properties of proteins govern their performance and behavior in food systems during processing, storage, and final food preparation as well as relate to sensory qualities. Factors affecting functional properties of food proteins can be classified as intrinsic, extrinsic, and process parameters, and those functional properties can be modified and improved (1). The tools available to modify the structure of proteins and hence alter their functional properties are chemical modifications, heat treatments, and enzymatic modifications. Particular attention has been devoted to enzymatic hydrolysis of proteins (2) because the resulting hydrolysates preserve and frequently enhance biological values, as well as achieve physicochemical properties superior to those of the original protein. Numerous reports on enzymatic modification of soy proteins to improve functional properties are available (3-7) and generally agree that soy protein can be modified to obtain improved functional properties that can be used in highly nutritional products such as beverages and infant formulas.Extruding-expelling (EE) is a relatively new process that combines extrusion and screw-pressing to recover oil from oilbearing seeds (8). A cooked semifluid extrudate is obtained in which the cell walls ...

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Enzymic modification of extruded soy protein concentrates as a method of obtaining new functional food components

Cited by 55 publications

References 26 publications

Modification of structural and functional properties of sunflower 11S globulin hydrolysates

Modification of structural and functional properties of sunflower 11S globulin hydrolysates

Characterizing the structural and surface properties of proteins isolated before and after enzymatic demulsification of the aqueous extract emulsion of peanut seeds

Enzymatic hydrolysis of extruded‐expelled soy flour and resulting functional properties

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