Functional properties of soy protein hydrolysates obtained by selective proteolysis

Tsumura, Kyosuke; Saito, Tsutomu; Tsuge, Keisuke; Ashida, Hiroko; Kugimiya, Wataru; Inouye, Kuniyo

doi:10.1016/j.lwt.2004.06.007

Cited by 189 publications

(142 citation statements)

References 20 publications

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“…Were et al (1997) observed that the emulsifying activity of papain-modified soy protein was not different from that of unmodified protein. The selective hydrolysis of β-conglycinin (by papain) or glycinin (by pepsin) from SPI resulted in poorer emulsifying ability at pH 5.5 and 7.0 when compared to control SPI (Tsumura et al 2005). The increased hydrolysis of peanut protein tended to decrease its emulsifying capacity (Jamdar et al 2010), and the same profile was observed for hemp protein isolate (Yin et al 2008), whey protein concentrates (Sinha et al 2007) and for ornate threadfin bream muscle (Nalinanon et al 2011).…”

Section: Foaming and Emulsifying Propertiesmentioning

confidence: 95%

“…The spontaneous behavior of proteins in aqueous solutions to adsorb to the air-water interface, causing the lowering of the interfacial (surface) tension, is of central importance for foaming properties (Foegeding et al 2006). Protein hydrolysis usually presents a positive effect on foaming capacity (Were et al 1997;Tsumura et al 2005;Sinha et al 2007;Jamdar et al 2010), since the generated peptides usually present an increased adsorption rate due to their faster diffusion to the interface when compared to the non-hydrolyzed proteins (Foegeding et al 2006;Martínez et al 2009). Emulsions, similarly to foams, are two-phase systems with one of the phases dispersed in an aqueous continuous one.…”

Section: Foaming and Emulsifying Propertiesmentioning

confidence: 99%

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Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

et al. 2014

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Soybean proteins are widely used as nutritional and functional food ingredients. This investigation evaluated through a 2 3 central composite design the effect of three variables (pH, temperature and enzyme/substrate (E/S) ratio) on the production of soy protein isolate (SPI) hydrolysates with a microbial protease. Soluble peptides, antioxidant activity, and foaming and emulsifying capabilities of the hydrolysates were analyzed. All variables, as well as their interactions, were significant for the soluble peptides content of SPI hydrolysates. Optimal conditions for obtaining soluble peptides were around 30-35°C, pH 6.5-9.5, and E/S ratios of 1,650-6,300 U g −1 . SPI hydrolysates produced at 30-45°C, pH 8.0-9.5, and E/S ratios of 4,000-8,000 U g −1 showed higher capacity to scavenge the 2,2′-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) radical. Models for soluble peptides and ABTS activity of hydrolysates were obtained. In the range studied, the variables had not significant influence on the ability of hydrolysates to scavenge the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical. SPI hydrolysates also presented reducing power and ability to chelate iron. Hydrolysis temperature was significant for the Fe 2+ -chelating ability of hydrolysates. Temperature of hydrolysis was significant for the foaming capacity of hydrolysates, with higher values observed at 45°C and 8,000 U g −1 . For emulsifying capacity, only E/S ratio presented a significant effect. Temperature and E/S ratio appeared to be more significant variables influencing the properties of the SPI hydrolysates. The results of this study indicate that specific hydrolysis conditions should be selected to obtain SPI hydrolysates with preferred characteristics.

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Section: Foaming and Emulsifying Propertiesmentioning

confidence: 95%

Section: Foaming and Emulsifying Propertiesmentioning

confidence: 99%

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

et al. 2014

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“…Solubility of SPHs was carried out over a wide range of pH value from pH 2.0 to pH 12.0 as described by Tsumura et al (2005). Briefly, 200 mg of protein hydrolysate sample were suspended in 20 ml of deionized distilled water and the pH of the mixture was adjusted to the desired values with 6 N HCl or 6 N NaOH solutions required.…”

Section: Solubilitymentioning

confidence: 99%

Composition, functional properties and in vitro antioxidant activity of protein hydrolysates prepared from sardinelle (Sardinella aurita) muscle

et al. 2011

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Composition, functional properties and in vitro antioxidative activities of protein hydrolysates prepared from muscle of sardinelle (Sardinella aurita) were investigated. Sardinelle protein hydrolysates (SPH) were obtained by treatment with crude enzyme preparations from Bacillus pumilus A1 (SPHA1), Bacillus mojavensis A21 (SPHA21) and crude enzyme extract from sardinelle (Sardinella aurita) viscera (SPHEE). The protein hydrolysates SPHA1, SPHA21 and SPHEE contained high protein content 79.1%, 78.25% and 74.37%, respectively. The protein hydrolysates had an excellent solubility and possessed interfacial properties, which were governed by their concentrations. The antioxidant activities of protein hydrolysates at different concentrations were evaluated using various in vitro antioxidant assays, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical method, reducing power assay, chelating activity, β-carotene bleaching and DNA nicking assay. All protein hydrolysates showed varying degrees of antioxidant activity. SPHA21 had the highest DPPH radical scavenging activity (89% at 6 mg/ml) and higher ability to prevent bleaching of β-carotene than SPHA1 and SPHEE (p<0.05). However, SPHEE exhibited the highest metal chelating activity (89% at 1 mg/ml) and the strongest protection against hydroxyl radical induced DNA breakage (p<0.05).

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“…Water-holding capacity (WHC) of the acidified gels was evaluated as per the Tsumura et al (2005) Fourier transform infrared spectroscopy, circular dichroism, and scanning electron microscope analyses. The analysed samples were prepared in KBr discs as per the Schneckenburger et al (2012) method.…”

Section: Methodsmentioning

confidence: 99%

Effects of transglutaminase-induced modification in the presence of oligochitosan of 1 kDa on the structure and gelling properties of caseinat

Song¹,

Zhao²

2016

Czech J. Food Sci.

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Milk gels have both traditional and high commercial value within the dairy industry (Schorsch et al. 2000;Siamand et al. 2014). Besides renneting, acidification of milk is the most routine way to form milk protein gels. Acidifying milk using glucono-δ-lactone (GDL) can slowly form structured gel products (Lucey 2004). Two major steps are involved in the formation of the acidified milk gels. In the first step, a collapse of the hairy brush of the casein micelles occurs, and the colloidal calcium and phosphate are then dissolved out of the casein micelle as a result of the protonation of ionised phosphate groups (Gaygadzhiev et al. 2009). Micellar structure is thus profoundly altered but without dissociation. In the second step, at a pH value about 5.0, casein precipitates isoelectrically, or under quiescent conditions it forms rather fragile gels (Lucey 2004). The balance between attractive and repulsive forces within protein molecules results in gel formation (Havea 2006;Rocha et al. 2009). Both intrinsic (e.g. amino acid compositions, molecular weights, hydrophobicity, etc.) and extrinsic (protein concentrations, pH value, temperature, metal ions, and ionic strengths) factors all show impacts on gelation and physiochemical properties of protein gels.During the last years, transglutaminase (TGase, EC 2.3.2.13) has been used to modify proteins via inducing protein cross-linking (between glutamine and lysine residues of the proteins) (Anema & Kruif 2012;Domagała et al. 2015). TGase-induced modification is able to form a more homogeneous gel network (Faergemand & Qvist 1997;Ercili-Cura et al. 2013), and thus improve water retention (Schorsch et al. 2000;Ercili-Cura et al. 2013) and texture (Ercili-Cura et al. 2010) of protein gels. 564Food Technology and Economy, Engineering and Physical Properties Czech J. Food Sci., 34, 2016 (6) Caseinate, transglutaminase (TGase), and an oligochitosan of 1 kDa were used to prepare a glycated and cross-linked caseinate (GC-caseinate), aiming to assess potential changes in both the structure and gelling properties of such caseinate. The results of Fourier transform infrared analysis revealed that only GC-caseinate contained saccharide portions in its molecules, evidencing TGase-induced caseinate glycation. Circular dichroism results showed that GC-caseinate possessed a more ordered secondary structure than caseinate. Other results also demonstrated that TGase-induced modification resulted in a lower gelation temperature of GC-caseinate (59°C vs. 68°C) and increased the final tan δ value (0.30 vs. 0.15) compared to caseinate during the development of acidified gels. In addition, the acidified gels from GC-caseinate were detected to have lower water holding capacity (0.720 vs. 0.781 g/g gels), expanded gel network, and larger pore sizes than those from caseinate. It is thus evidenced that the used TGase-induced modification could confer caseinate with ordered secondary structure, expanded gel network but lower water holding capacity.

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Functional properties of soy protein hydrolysates obtained by selective proteolysis

Cited by 189 publications

References 20 publications

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

Composition, functional properties and in vitro antioxidant activity of protein hydrolysates prepared from sardinelle (Sardinella aurita) muscle

Effects of transglutaminase-induced modification in the presence of oligochitosan of 1 kDa on the structure and gelling properties of caseinat

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