• Korean Journal of Food Science and Technology
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• v.22 no.3
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• pp.350-356
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• 1990

Functional properties such as nitrogen solubility, emulsifying property, foaming property, and water and oil absorption of sesame and perilla protein isolates were determined at pH range of 2-10 and ionic strength of 0-0.5M NaCl. Nitrogen solubility of protein isolates in distilled water showed minimum value at pH6.0 in sesame and at pH 4.0 in perilla and soybean protein isolates, and significantly increased above pH 8.0 in all samples. Addition of 0.1M NaCl solution increased nitrogen solubility, however, decreased in 0.5M NaCl solution. Emulsion activities of all the protein isolates showed minimum value at pH 4.0 and increased in 0.1M NaCl solutions while it was reduced in 0.5M NaCl solutions. The perilla protein isolate showed higher emulsion activity than that of soybean and sesame protein isolates at above pH 6.0. Foaming capacities of sesame and perilla protein isolates were lower than soybean protein isolate and generally all of the samples showed higher profiles in NaCl solutions. The foaming stability of soybean isolate decreased abruptly in 10min, while it was slowly decreased for sesame and perilla isolates during initial 30 min. Oil absorption capacity of perilla protein isolate was higher than that of sesame and soybean protein isolates. Water absorption capacity was similar among the three samples studied.

• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.2
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• pp.67-70
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• 1998

In order to understand the influence of ferroxidase center on the protein assembly and solubility of tadpole ferrin, three mutant plasmids, pTH58K, pTH61G, and pTHKG were constructed with the aid of site-directed mutagenesis and mutant proteins were produced in Eshcerichia coli. Mutant ferritin H-subunits produced by the cells carrying plasmids pTH58K and pTHKG were active soluble proteins, whereas the mutant obtained from the plasmid pTH61G was soluble only under osmotic stress in the presence obtained from the plasmid pTH61G was soluble only under osmotic stress in the presence of sorbitol and betaine. Especially, the cells carrying pTH61G together with the plasmid pGroESL harboring the molecular chaperone genes produced soluble ferritin. The mutant ferritin H-subunits were all assembled into ferritin-like holoproteins. These mutant ferritns were capable of forming stable iron cores, which means the mutants are able to accumulate iron with such modified ferroxidase sites. Further functional analysis was also made on the individual amino acid residues of ferroxidase center.

• Korean Journal of Food Science and Technology
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• v.23 no.3
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• pp.286-290
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• 1991

Phytic acid known as an antinutritional facfor was studied for its effect on the solubility and digestibility of high-phytate and low-phytate soy protein isolates (SPI) obtained by two different methods of pH adjustment. Phytic acid content was 2.48% in high-phytate SPI and 0.72% in low-phytate SPI. Solubility of soy proteins was higher in low-phytate SPI than in high-phytate SPI at all pH values tested and it was lowered by adding more phytic acid to result in precipitation of the proteins. The inhibitory effect of phytic acid toward pepsin digestion of SPI increased by the increasing amount of phytic acid added and its effect was slightly higher in high-phytate SPI than in low-phytate SPI.

• Food Science of Animal Resources
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• v.41 no.5
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• pp.869-882
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• 2021

Sodium chloride (NaCl) replacement with calcium chloride (CaCl₂) effect on protein solubility, proteolytic enzyme and quality characteristics of a chicken soup prepared from spent hen (SH) chicken were investigated. By means of immerse marination prior to cooking, a total of 60 skinless SH breast meat were randomly allocated into ten groups admitted to treatments with marinade solution containing sodium tripolyphosphate (STPP) and reduced percentage of NaCl with CaCl₂ at 0%, 25%, 50%, 75%, and 100% at 4±2℃ for 20 h. STPP was adjusted to 0.5% for all treatments and NaCl replacement at 0% was used as control. The different methods, particularly boiling at 100℃ and retorting at 121℃, 1.5 kgf/cm² for 60 minutes, were applied following marination. An upregulation of cathepsin-B and caspase-3 enzymes were a consequences from a higher percentage of CaCl₂ within meat environment. Accordingly, modified the protein solubility in particular the myofibrillar and total protein solubility. In addition, a significant increase in water holding capacity (WHC), pH value, myofibril fragmentation index (MFI), and moisture content was obtained due to salt replacement (p<0.05). Limited effect was observed for shear force value, collagen content and cooking yield. Eventually, this study implied that although protelytic enzyme and protein solubility was upregulated by the replacement of NaCl with CaCl₂ at >75%, extensive effect on texture properties was not observed. Therefore, NaCl replacement at 75% could be a promising strategy for quality improvement of SH chicken soup.

• Korean Chemical Engineering Research
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• v.47 no.5
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• pp.624-629
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• 2009

It is the most important step to screen soluble and insoluble proteins when we attempt to improve the solubility of recombinant proteins through directed evolution approach. Here we show that the solubility of a recombinant protein in vivo can be examined by expressing the recombinant protein with beta-lactamase as a fusion partner. First we constructed an expression system which can produc a fusion protein with the C-terminal of beta-lactamase. Two soluble proteins, i.e. adenine deaminase and aspartate aminotransferase, and insoluble GlcNAc-2-epimerase were cloned into the developed expression vector, respectively. We investigated the effect of the expression of the three recombinant fusion proteins on the growth of E. coli, and confirmed that the solubilities of the recombinant proteins correlated with cell growth rates.

• Food Science of Animal Resources
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• v.39 no.2
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• pp.296-308
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• 2019

Although the yellow mealworm (Tenebrio molitor L.) is a promising alternative protein source, the effects of processing conditions on functional properties are unclear. In this study, a protein extract of yellow mealworm larvae (PEYM) was subjected to different heat temperature ($55^{\circ}C$, $75^{\circ}C$, and $95^{\circ}C$) with different time (20, 40, and 60 min) to evaluate the functional properties and protein oxidation. Different heat temperature treatment significantly affected the exposure of surface hydrophobicity of the proteins and protein molecule aggregation, which reached maximum levels at $95^{\circ}C$ for 60 min. Protein oxidation was inversely proportional to the temperature. Both the highest carbonyl value (1.49 nmol/mg protein) and lowest thiol value (22.94 nmol/mg protein) were observed at $95^{\circ}C$ for 60 min. The heating time-temperature interaction affected several functional properties, including solubility, emulsifying potential, and gel strength (GS). Solubility decreased near the isoelectric point (pH 5 to 6). As the temperature and heating time increased, emulsifying properties decreased and GS increased. The oil absorption capacity and foaming properties decreased and the water absorption capacity increased. These results confirmed that PEYM is a suitable source of proteins for processing and applications in the food industry.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.4
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• pp.587-594
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• 2010

To develop commercially available food protein hydrolysates, the effects of different types of enzymes and substrates on bitterness and solubility of partially hydrolyzed food proteins were investigated. Four types of proteins (casein, isolated soy protein (ISP), wheat gluten, and gelatin) and five types of proteolytic enzymes (a microbial alkaline protease (alcalase), a microbial neutral protease (neutrase), papain, bromelain, trypsin) were used. To profile the pattern of hydrolysis, the degree of hydrolysis (DH) were monitored during 180 min of reaction time by pH-stat method. Casein showed the highest susceptibility to hydrolysis for all five proteases compared to those of ISP, gluten, and gelatin. In addition, the bitter intensity and solubility (nitrogen soluble index, NSI) of each protein hydrolysate were compared at DH 10%. Bitterness and solubility of protein hydrolysates were highly affected by DH and the types of enzymes and substrates. At DH=10%, casein hydrolysate by trypsin, ISP and gluten hydrolysates by either bromelain or neutrase, and gelatin hydrolysates by the five proteases tested in this study were highly soluble and less bitter.

• Applied Biological Chemistry
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• v.29 no.2
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• pp.212-218
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• 1986

Proteins in Korean rapeseeds, as in many other plantseeds, are usually bound to phytate molecules. These phytate-bound proteins are of little value as foodstuffs because of their poor solubility in digestive systems. Therefore it is necessary to remove phytates from proteins in order to convert these proteins io a useful foodstuff. In the work, an efficient procedure for removal of phytates from defatted Korean rapeseed was found. The influence of pH on the solubility of protein and phytate of rapeseed flour showed that the former was the lowest at pH 5.0 and began to increase as pH further raised. Meanwhile, the latter was the highest at pH 6.0, however, it was decreased abruptly at alkaline pH, especially to content of 1.3% at pH 11.5. The solubility cf protein was relatively high in NaCl aqueous solution at $pH\;6.0{\sim}8.0$, and did not male any noticeable difference depending on NaCl concentration. On the other hand, the solubility of phytate was high at pH of below 6.0 showing an abrupt decrease at pH of above 6.0. The solubility of protein in $CaCl_2$ aqueous solution was highest at $pH\;6.0{\sim}8.0$, however, there was no significant change at the whole range of tested pH of the solution. A maximum solubility of phytate was shown at $pH\;3.0{\sim}4.0$. And it was decreased abruptly at a higher pH of the above range and also decreased at a lower pH with higher $CaCl_2$ concentration. The solubility of phytate in $Na_2SO_3$ aqueous solution was highest at $pH\;5.0{\sim}8.0$. As the concentration goes up the maximum value of solubility was found to move to higher pHs. Depending on the concentration of $Na_2SO_3$, the decreasing pattern was changed in an alkaline solution. The solubility of phytate in the solution containing low concentration of $Ca^{2+}$ ion was low in all treatments at pH of above 7.0 and showed the maximum value at low pH as $Ca^{2+}$ ion concentration increases. The solubility of protein at pH 11.5 showed the highest value in $1mM\;Ca^{2+}$ ion solution.

• Food Science of Animal Resources
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• v.43 no.3
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• pp.491-501
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• 2023

Comparing the effects of sodium tripolyphosphate (STPP) concentrations of 0.2% and 0.4% on beef semitendinosus is the objective of the current investigation. The samples were cooked at varied temperatures (45+60℃ and 45+70℃) and times (1.5+1.5 h and 3+3 h) using staged cooking. The colour properties, cooking loss, water retention, shear force, water-holding capacity, sarcoplasmic, and myofibrillar solubility, and total collagen were investigated. The cooking time and temperature affected the water-holding capacity, cooking loss, CIE L^*, CIE a^*, CIE b^*, myofibrillar, and sarcoplasmic solubility, with lower temperature and short time having the lower detrimental effect. However, the significant effect can be intensified after the addition of STPP with higher water-holding capacity and tender meat obtained with 0.4% phosphate concentration at any cooking conditions. The STPP lowered the collagen content and increased the protein solubility of myofibrillar and sarcoplasmic, which this degradation is used as a good indicator of tenderness.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.19 no.2
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• pp.100-108
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• 1986

This study was carried out in order to investigate protein cross-linking in freeze-dried meat of flounder (Limanda herzensteini). Changes in solubility or extractability of proteins and electrophoretic patterns of the extracted proteins were determined to monitor the cross-linking during the storage of freeze-dried meat. Development of nonenzymatic browning and the loss of in vitro protein digestibilily were also measured to assess their influences on the changes of functional and nutritional properties of proteins. In addition, the effects of lysine added, and removal of fat and water extractives were also mentioned. The extractability of protein decreased upon storage time and temperature, and the loss of solubility of myosin was evident. In case of the samples stored at $5^{\circ}C$ for 150 days, the extractability of protein decreased $26.4\%$, while that of the samples stored at $20^{\circ}C$ for 60 days decreased about $39.7\%$. And it was noted that the loss of solubility of myosin was $68.3\%$ and $98.1%$ for the same storage conditions, respectively. It was noteworthy that the samples treated with $L-lysine{\cdot}HCl$ seemed to prevent more or less the loss of protein solubility, in that, even stored at $20^{\circ}C$ for 120 days, revealed only $57.03\%$ decrease. The nonenzymatic browning was proceeded with the increase of storage temperature, especially, in the samples treated with glucose. This suggests that the decrease in extractibility of myosin was accompanied by the extent of browning. But the browning was retarded in defatted samples. The in vitro apparent protein digestibility was also higher in the samples defatted or water extracted. It was suggested from these results that changes in properties of proteins in freeze dried fish meat were led by the protein cross-linking which was attributed to Maillard type of reactions and protein-lipid interactions.