Improvement of protein gel by physical and enzymatic treatment

Kitabatake, Naofumi; Doi, Etsushiro

doi:10.1080/87559129309540974

Cited by 25 publications

(21 citation statements)

References 44 publications

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“…In general, the formation of SPI film and gel structures involves covalent disulfide bonds as well as hydrophobic interactions and hydrogen bonds (Fukushima and Van Buren, 1970;Farnum et al, 1976;Doi and Kitabatake, 1989). SDS does not cleave disulfide bonds, but it prevents hydrophobic associations among protein molecules (Fukushima and Van Buren, 1970;Kitabatake and Doi, 1993). This is accomplished through attachment of the hydrophobic (non-polar) portions of the SDS molecules onto hydrophobic amino acid residues (Krull and Wall, 1969).…”

Section: Tensile Propertiesmentioning

confidence: 99%

“…Ionic surfactants, such as sodium dodecyl sulfate (SDS), are powerful denaturing and dissociating agents for proteins (Graveland et al, 1979;Cheftel et al, 1985). Strength reduction, and even re-solubilization, of protein gels in SDS buffers has been reported (Kitabatake and Doi, 1993;McClements et al, 1993;Kiosseoglou et al, 1999). Therefore, incorporation of SDS into protein-based film-forming solutions would be expected to affect the structure and properties of cast protein films.…”

Section: Introductionmentioning

confidence: 99%

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Sodium dodecyl sulfate treatment improves properties of cast films from soy protein isolate

Rhim

Gennadios

Weller

et al. 2002

Industrial Crops and Products

105

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The manufacture of edible/biodegradable films or coatings can potentially add value to soy protein. This study was conducted to determine the effect of sodium dodecyl sulfate (SDS) on selected physical properties of glycerin-plasticized soy protein isolate (SPI) films. Films were cast from heated (70 °C for 20 min), alkaline (pH 10) aqueous solutions of SPI (5 g/100 ml water), glycerin (50% w/w of SPI), and SDS (0, 5, 10, 20, 30, or 40% w/w of SPI). Tensile strength (TS), elongation at break (E), moisture content (MC), total soluble matter (TSM), water vapor permeability (WVP), and color values (L, a, and b) were determined after conditioning film specimens at 25 °C and 50% relative humidity (RH) for 2 days. SDS reduced (P < 0.05) film TS by as much as 43% for films with 40% SDS (6.2 vs. 10.9 MPa for control SPI films). In contrast, film E increased (P < 0.05) notably with addition of SDS even at 5%. Films with SDS had smaller (P < 0.05) MC and larger (P < 0.05) TSM values than control SPI films. Films containing 10% or more SDS had lower WVP values than control SPI films by as much as 50%. Increased yellowness, evidenced by greater (P < 0.05) + b color values, was noted for films with high amounts (20, 30, or 40%) of SDS. Changes in tensile, solubility, and water vapor barrier properties of SPI films due to the addition of SDS were largely attributed to disruption of hydrophobic associations among neighboring protein molecules as the non-polar portions of the SDS molecules attached onto hydrophobic amino acid residues within the film structure. It was demonstrated that adding anionic surfactant SDS to film-forming solutions prior to casting could greatly modify the properties of SPI films. In particular, SDS improved the water vapor barrier ability and the extendibility of SPI films, both desirable attributes when assessing the potential of such films for packaging applications.

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Section: Tensile Propertiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Sodium dodecyl sulfate treatment improves properties of cast films from soy protein isolate

Rhim

Gennadios

Weller

et al. 2002

Industrial Crops and Products

105

View full text Add to dashboard Cite

show abstract

“…Whey proteins are widely used as structural building blocks in food products [1][2][3]; their ability to denature and aggregate into a three-dimensional network makes them especially suitable as gelling agents and texture modifiers. Most frequently the gelation of whey proteins is induced by heating, although cold-set gels can also be obtained by the addition of salts or by using high pressure or enzymatic treatments [4][5][6][7]. The main molecular interactions involved in the association and cross-linking of denatured whey proteins are hydrophobic forces and covalent bonding via intermolecular disulfide linkages [8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

Microstructure of β-lactoglobulin-stabilized emulsions containing non-ionic surfactant and excess free protein: Influence of heating

Kerstens

Murray

Dickinson

2006

Journal of Colloid and Interface Science

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“…When the interaction between denatured protein molecules is restricted and the coagulation of protein molecules is inhibited, a linear aggregate of denatured protein molecules is formed (Kitabatake and Doi, 1993). Hydrophobic interaction seems to be important in the linking of molecules to form the aggregate.…”

Section: Introduction Milkmentioning

confidence: 98%

Simple and Rapid Method for Measuring Turbidity in Gels and Sols from Milk Whey Protein

Kitabatake

Doi

Kinekawa

1994

Journal of Food Science

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Protein isolates prepared from acid whey concentrate and cheese whey concentrate, and P-lactoglobulin were studied. Turbidity of samples was measured using a 96-well microplate and a microreader. This method allowed many (>lOO) small samples (< 250 pL) to be treated at the same time. At low ionic strength and at neutral to alkaline pH, samples were transparent after heating. Transparent gels could also be prepared in this region with a small amount of NaCl.

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Improvement of protein gel by physical and enzymatic treatment

Cited by 25 publications

References 44 publications

Sodium dodecyl sulfate treatment improves properties of cast films from soy protein isolate

Sodium dodecyl sulfate treatment improves properties of cast films from soy protein isolate

Microstructure of β-lactoglobulin-stabilized emulsions containing non-ionic surfactant and excess free protein: Influence of heating

Simple and Rapid Method for Measuring Turbidity in Gels and Sols from Milk Whey Protein

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