Taste Evaluation for Peptides in Protein Hydrolysates from Soybean and Other Plants

Maehashi, Kenji; Arai, Soichi

doi:10.1007/978-3-662-04857-3_4

Cited by 5 publications

(3 citation statements)

References 49 publications

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“…The sugars use are monosaccharides such as fructose and glucose, disaccharides such as sucrose and trehalose, and sugar alcohol like xylitol, lactitol, mannitol, sorbitol, maltitol, and erythritol (Araki 2000). Enzymatic debittering methods using different enzymes, such as exopeptidases (Lovsin-Kukmanand and others 1996;Maehashi and Arai 2002;Raksakulthai and Haard 2003), aminopeptidase from the edible basidiomycete Grifola frondosa (Nishiwaki and others 2002), have also been developed. These studies indicate that as the incubation time elapses, the amount of free amino acids released increases and the bitterness of the reaction mixtures decreases.…”

Section: Sensory Aspectsmentioning

confidence: 99%

A New Frontier in Soy Bioactive Peptides that May Prevent Age-related Chronic Diseases

Wang

Mejía

2005

Comp Rev Food Sci Food Safety

333

182

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During gastrointestinal digestion or food processing of proteins, small peptides can be released and may act as regulatory compounds with hormone‐like activities. Numerous biologically active peptides (bioactive peptides) have been identified. Most bioactive peptides are derived from milk and dairy products, with the most common being angiotensin converting enzyme inhibitory peptides. Soybean protein and soybean derived peptides also play an important role in soybean physiological activities, particularly those related to the prevention of chronic diseases. However, the bioactive potential of soybean derived bioactive peptides is yet to be fully appreciated. After a general introduction of approaches and advances in bioactive peptides from food sources, this review focuses on bioactive peptides derived from soybean proteins and their physiological properties. Technological approaches to generate bioactive peptides, their isolation, purification, characterization, and quantification, and further application in food and drug design are also presented. Safety concerns, such as potential toxicity, allergenicity, and sensory aspect of these peptides are likewise discussed.

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Section: Sensory Aspectsmentioning

confidence: 99%

A New Frontier in Soy Bioactive Peptides that May Prevent Age-related Chronic Diseases

Wang

Mejía

2005

Comp Rev Food Sci Food Safety

333

182

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“…However, it is important to conduct consumer studies to evaluate the acceptance of food products containing protein hydrolysates, as this largely depends on the specific food matrix used. Moreover, masking flavors may be necessary for many plant proteins and protein hydrolysates to achieve desirable sensory attributes [ 44 , 45 , 46 , 47 ]. Thus, additional research is needed to determine effective strategies for mitigating the bitter taste and ensuring the acceptability of food products incorporating protein hydrolysates.…”

Section: Resultsmentioning

confidence: 99%

Physical and Oxidative Stability of Emulsions Stabilized with Fractionated Potato Protein Hydrolysates Obtained from Starch Production Side Stream

et al. 2023

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This work studies the emulsifying and antioxidant properties of potato protein hydrolysates (PPHs) fractions obtained through enzymatic hydrolysis of potato protein using trypsin followed by ultrafiltration. Unfractionated (PPH1) and fractionated (PPH2 as >10 kDa, PPH3 as 10–5 kDa, PPH4 as 5–0.8 kDa, and PPH5 as <0.8 kDa) protein hydrolysates were evaluated. Pendant drop tensiometry and dilatational rheology were applied for determining the ability of PPHs to reduce interfacial tension and affect the viscoelasticity of the interfacial films at the oil–water interface. Peptides >10 kDa showed the highest ability to decrease oil–water interfacial tension. All PPH fractions predominantly provided elastic, weak, and easily stretchable interfaces. PPH2 provided a more rigid interfacial layer than the other hydrolysates. Radical scavenging and metal chelating activities of PPHs were also tested and the highest activities were provided by the unfractionated hydrolysate and the fractions with peptides >5 kDa. Furthermore, the ability of PPHs to form physically and oxidatively stable 5% fish oil-in-water emulsions (pH 7) was investigated during 8-day storage at 20 °C. Our results generally show that the fractions with peptides >5 kDa provided the highest physicochemical stability, followed by the fraction with peptides between 5 and 0.8 kDa. Lastly, promising sensory results with mostly mild attributes were obtained even at protein concentration levels that are higher than needed to obtain functional properties. The more prominent attributes (e.g., bitterness and astringency) were within an acceptable range for PPH3 and PPH4.

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“…Several studies have been performed on the hydrolysis of soybean protein and the development of bioactive peptides from soybean meal [ 40 , 51 , 52 ], soybean protein concentrate [ 39 , 53 ], soybean protein isolate (SPI) [ 53 , 54 ], soybean flour [ 55 , 56 ] and soybean protein hydrolysate [ 57 , 58 ] through different serine proteases, which generally creates peptides with bitter taste [ 59 , 60 ]. Applications of cysteine proteases, such as papain (EC 3.4.22.2) from papaya latex, bromelain from pineapple stem (EC 3.4.22.32) and fruit (EC 3.4.22.33), ficin (EC 3.4.22.3) from the latex of fig, zingibain (EC 3.4.22.67) from ginger, actinidin (EC 3.4.22.14) from kiwifruit and aspartic protease cardosin (E.C.3.4.23) from tobacco in the food industry are acceptable because they do not create undesirable organoleptic properties [ 61 , 62 ].…”

Section: Introductionmentioning

confidence: 99%

Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives

et al. 2022

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The objective of the investigation was to understand the biochemical activities of hydrolysate of soybean milk protein (SMP). Hydrolysis was carried out by different concentrations of papain (0.008 g·L−1, 0.016 g·L−1, 0.032 g·L−1 and 0.064 g·L−1). The antioxidant capacity was measured by the ferric-reducing ability of plasma (FRAP) and 2,2-Diphenyl-1-picrylhydrazyl (DPPH) assays. The anti-angiotensin activity of hydrolysate was measured by the recombinant angiotensin converting enzyme and substrate Abz-FRK(Dnp)-P. The contributions of the Kunitz trypsin inhibitor (KTI) and Bowman–Birk inhibitor (BBI) on antigenicity, and the in vitro digestion of papain-hydrolyzed SMP were studied. Rabbit polyclonal anti-KTI and anti-BBI antibodies together with peroxidase-labelled goat anti-Rb IgG secondary antibody were used to identify the antigenicity of KTI and BBI in unhydrolyzed and papain-hydrolyzed SMP. The antioxidant capacity and anti-angiotensin activity of SMP were increased after the papain hydrolysis of SMP. The KTI- and BBI-specific antigenicity were reduced in SMP by increasing the concentration of papain. However, there was interaction between papain-hydrolyzed SMP and trypsin in native gel, while interaction with chymotrypsin was absent. The interaction between trypsin and SMP was reduced due to the hydrolysis of papain in a concentration-dependent manner. According to the in vitro gastrointestinal digestion simulation protocol (Infogest), the digestibility of SMP was not statistically increased.

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Taste Evaluation for Peptides in Protein Hydrolysates from Soybean and Other Plants

Cited by 5 publications

References 49 publications

A New Frontier in Soy Bioactive Peptides that May Prevent Age-related Chronic Diseases

A New Frontier in Soy Bioactive Peptides that May Prevent Age-related Chronic Diseases

Physical and Oxidative Stability of Emulsions Stabilized with Fractionated Potato Protein Hydrolysates Obtained from Starch Production Side Stream

Hydrolysis of Soybean Milk Protein by Papain: Antioxidant, Anti-Angiotensin, Antigenic and Digestibility Perspectives

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