• Applied Biological Chemistry
• /
• v.40 no.5
• /
• pp.404-408
• /
• 1997

Enzymatically hydrolyzed vegetable protein (eHVP) was produced from soy protein using proteases, and the physicochemical properties were examined. Soy protein hydrolysate of 6% protein and 50% degree of hydrolysis was useful for the base of savory ingredients. The Maillard-reacted and flavoring compound-added hydrolysate had improved flavor. It was for enzymatically hydrolyzed soy sauces and dehydrated seasonings. ISP hydrolysate of low molecular weight $(MW{\sim}250)$ and high protein content (85%) was suitable for special uses such as infant diets, sports nutrition, and medical diets. The eHVP gave no limitation of dosage in the formulation as a flavor enhancer. The byproduct of protein hydrolysis was found to have high content of fiber (21%) and to have potential for the use as dietary fiber or bulking agents.

• The Korean Journal of Food And Nutrition
• /
• v.19 no.3
• /
• pp.243-253
• /
• 2006

This study was designed to investigate the feasibility of utilizing concentrates of sunmul(soybean curd whey), the waste by-product of soybean curd processing, as functional food ingredients. Sunmul was concentrated by nanofiltration fo11owing ultrafiltration and then freeze-dried. The oil adsorption capacity of the nanofiltraion(NF) powder(97.33g/100g) was similar to that of sunmul powder(94.17g/100g), but was lower than that of ISP(isolated soy protein). However, the water holding capacity of NF powder could not be determined because the NF powder completely dissolved in water. The protein solubilities of sunmul powder and ISP in distilled H$_{2}$O, 0.1M and 0.5M NaCl were lowest at pH 4.0 and increased at more acidic or alkaline conditions. However, the protein solubility of NF powder was at its minimum at pH 6.0 and increased at more acidic or alkaline conditions. Emulsifying activity indexes of NF powder in 4% and 6% solution were minimal at pH 4.0 and 6.0, respectively, which were 3 to 8 times lower than that of sunmul powder. The emulsion stability of 4% sunmul solution was lowest at pH 4.0, but that of NF powder was highest at pH 5.0 and decreased at more acidic or alkaline conditions at all concentrations of solution. The total free amino acid contents of protein in sunmul, and NF power were 99.07 and 2,110.10mg%, respectively, and NF powder exhibited especially high threonine content. Rapid viscosity analysis of dough with 1 to 5% added NF powder demonstrated that all of the peak and final viscosities decreased with increasing NF powder concentration compared to the control.

• Korean Journal of Food Science and Technology
• /
• v.32 no.1
• /
• pp.161-167
• /
• 2000

The protease produced by a newly isolated Aspergillus wentti from Korean traditional Meju was purified and characterized. The optimal medium composition and culture conditions for maximum protease production were ; bran :1% glucose solution =1 : 1, pH 9.0, $30^{\circ}C$, and 4 days of fermentation. Protease was purified by QAE-Sephadex, SP-Sephadex ion exchange chromatography and Sephadex G-100 chromatography. The specific activity and the purification fold of the purified enzyme were 213 unit/mg protein and 27.3, respectively. The molecular weight of purified protease was found to be 32 kDa by SDS-PAGE. Km and Vmax value's for hammastein milk casein were $3.049{\times}10^{-4}\;M\;and\;151.1\;{\mu}g/min$, respectively. Kinetic parameters showed that the enzyme has higher affinity to casein than isolated soybean protein, hemoglobin and bovine serum albumin. Optimal pH and temperature for reaction of the purified enzyme were 9.0 and $50^{\circ}C$, respectively. The enzyme was stable at pH 4.0-11.0, below $40^{\circ}C$, and the activity was not stimulated by metal ions. 1mM phenylmethylsulfonyl fluoride inhibited the enzyme activity by 98.5%. It means that the enzyme is one of serine protease.

• Food Science and Preservation
• /
• v.30 no.5
• /
• pp.875-884
• /
• 2023

In this study, the quality characteristics of texturized vegetable proteins (TVP) produced from defatted soy flour (DSF) were analytically compared with those of texturized vegetable proteins produced with isolated soy protein (ISP) and non-defatted soy flour (SF). The base raw material formulation consisted of 50% soy proteins, 30% gluten, and 20% corn starch. A cooling die-equipped extruder was used with a barrel temperature set at 190℃ and screw rotation speed of 250 rpm. With respect to the hardness of isolate soy proteins, that of soy flour and defatted soy flour was 22.4% and 68.8%, respectively, and gumminess was 17.6% and 44.3%, respectively. Defatting increased chewiness, shear strength, and springiness. Moisture content was higher in soy flour than in defatted soy flour, while there were no significant differences in terms of water absorption and turbidity. The pH was higher with soy flour than with defatted soy flour. Concerning color, the L and b values were higher with soy flour, while the a value was higher with defatted soy flour. These results suggest that defatting soybeans can improve the quality of plant-based proteins. Further research is needed to address the quality differences from those of isolated soy proteins.

• Korean Journal of Food Science and Technology
• /
• v.47 no.6
• /
• pp.772-778
• /
• 2015

Hydrolysis of isolate soybean protein (ISP) using subcritical water (SCW) was conducted to study the feasibility for producing protein hydrolyzate. SCW hydrolysis of SPI suspension (5-15%) was conducted in an electrically heated batch reactor (2 L). The effects of temperature (230 to $270^{\circ}C$) and holding time (10 to 50 min) on the degree of hydrolysis (DH) and the production of amino acids were studied by surface response method. The DH was determined by derivatizing the hydrolyzates with ortho-phthalaldehyde (OPA) solution. It was confirmed that reaction temperature and holding time affected the hydrothermolysis of soybean protein. However, the holding time was less effective on amino acid yield when the temperature was higher than $230^{\circ}C$. In order to achieve optimal yields of amino acids exceeding 43%, the temperature should be within the range between 256 and $268^{\circ}C$ with holding time from 29 to 41 min, respectively. A maximum estimated amino acid yield of 43.5% was obtained at $268^{\circ}C$ for 35 min.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.56 no.2
• /
• pp.162-173
• /
• 2023

Four roe protein isolates (RPIs) from olive flounder Paralichthys olivaceus roes (OFR) were recovered by isoelectric solubilization (pH 11 and 12) and precipitation (pH 4.5 and 5.5) and investigated for their food characteristics. RPIs contained 4.5-9.6% moisture, 64.1-69.5% protein, 16.1-19.8% lipid, and 1.0-3.9% ash. The protein yields of RPIs ranged from 50.1 to 56.8%, which was significantly different depending on the recovery conditions. A difference was observed in the SDS-PAGE protein band (25-100 kDa) between the alkaline solubilization at pH 11 (RPI-1 and 2) and pH 12 (RPI-3 and 4). The major amino acids of RPIs were Leu, Lys, Asp, Glu and Ala and major mineral components were sulfur, sodium, phosphorus, and magnesium, which were significantly different from OFR (P<0.05). Additionally, the lead and cadmium content was below the chemical hazard standard of the Korean food standards code. The Hunter color and whiteness of RPIs also showed significant differences according to the treatment conditions of the ISP process (P<0.05). This suggests that protein isolates recovered from olive flounder roes have high potential as nutritional supplements.