• Asian-Australasian Journal of Animal Sciences
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• v.11 no.6
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• pp.725-731
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• 1998

Nine crossbred female pigs fitted with the bladder catheters were used to investigate the effects of dietary protein form on the efficiency of absorbed nitrogen for nitrogen retention in growing pigs. Combinations of the main protein sources were corn-soybean meal (CSM; slow + slow absorption rate form), corn-hydrolyzed casein (CAS; slow + rapid absorption rate form) and corn-porcine plasma (CPL; slow + intermediate absorption rate form). All experimental diets were formulated to be isonitrogenous (CP 11%) and isocaloric (3.5 Mcal/kg) and synthetic amino acids were added to the diet as required to maintain an equivalent amino acid profile among diets. Fecal digestibility of nitrogen was not different among treatments (p > 0.10). Ingested nitrogen was absorbed with an apparent efficiency of 82% to 84%. Mean nitrogen retention in pigs fed the CSM diet was as high as for pigs fed the CPL diet (0.74 g N/kg $BW^{0.75}$ per d), which was higher than the N retention rate in pigs fed CAS diet (0.68 g/kg $BW^{0.75}$ per d; P < 0.05). Apparent biological values (ABV = 100 ${\times}$ N retention/absorbed nitrogen) were 63.3%, 58.0% and 61.6% for CSM, CAS, and CPL groups, respectively (p < 0.05). There was no difference in mean energy digestibility among treatments. The efficiency of absorbed lysine utilization was significantly different among treatments (p < 0.05). Pigs fed the CAS diet were inferior to counterparts on the other diets in utilizing absorbed lysine. The ratios of free (and small peptide-bound) to protein-bound amino acids in CSM diet differed considerably from the CAS diet. This may affect the efficiency of amino acids utilization for nitrogen retention if hydrolyzed and intact amino acid pools reach the blood at different times.

• Journal of Plant Biology
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• v.39 no.3
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• pp.173-177
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• 1996

A novel calcium binding protein (CaBP) was purified to electrophoretic homogeneity from Dunaliella salina. In the course of purification experiment, this CaBP was identified as a monomer and its molecular weight was about 21 kDand isoelectric point (pI) value was about 4.1 using isoelectrofocusing. This CaBP was able to bind Ca2+ even in the pressence of an excess MgCl2 and KCI both in solution. In the SDS-PAGE, the Ca2+-bound form was slower than the Ca2+-free form in the nondenaturing PAGE. This means that the CaBP undergoes conformational change in the Ca2+-bound condition. Furthermore, UV absorption spectrum and fluorescence intensity of this CaBP was investigated. UV absorption peak was appeared at about 258 nm and decreased somewhat in Ca2+-bound condition. In the measurement of fluorescence, maximum intensity was appeared at 303 nm and decreased in Ca2+-bound state, similarly as UV absorption spectrum. These show distinct changes upon Ca2+-binding, which indicate of structural and/or dynamic changes largely reminiscent of other members of the EF-hand Ca2+-binding protein family.

• Journal of Integrative Natural Science
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• v.9 no.4
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• pp.249-254
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• 2016

This study evaluated the physical and optical characteristics of hydrophilic ophthalmic polymer with addition of 2-methacryloyloxyethyl phosphorylcholine in the basic hydrogel ophthalmic lens material, and in particular, the utility of 2-methacryloyloxyethyl phosphorylcholine as an ophthalmic contact lens material for ophthalmologic devices was investigated. In this study 2-methacryloyloxyethyl phosphorylcholine were used as additives. For the preparation of hydrogel lens 2-hydroxyethyl methacrylate, methyl methacrylate, acrylic acid and a cross-linker EGDMA were copolymerized in the presence of AIBN as an initiator. The physical properties of the produced polymers were measured as followings. The refractive index of 1.433~1.393, water content of 35.95~53.16%, contact angle of $70.6{\sim}51.24^{\circ}$, UVB transmittance of 81.2~82.4%, UV-B transmittance of 81.2~82.4% and visible transmittance of 91.4~92.2% were obtained. Also, in case of protein absorption, the measurement showed that absorbance of Reference and MPC-10 sample was 0.2598 and 0.2250 respectively. Based on the results of this study, ophthalmic lens material containing 2-methacryloyloxyethyl phosphorylcholine is expected to be used usefully as a material for high wettability and inhibitor of protein adsorption for ophthalmic hydrogel lens.

• Journal of Ginseng Research
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• v.7 no.1
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• pp.23-36
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• 1983

This study was devised to observe the nutritional effects of the diets supplemented with the leaf or trunk in rats. The male albino rats (110 heads), Sprague-Dowley strain weighing 75g to 79g, were used as the experimental aninl mils. The animals were divided into twelve diet groups and maintained with corresponding diet for 40 days, and then sacrificed. The growth rate, the consumption and efficiency ratios of the food and protein, the absorption rates of carbohydrate, lipid and protein, and the utilization rates of energy were determined during the feeding term. The results obtained are summarized as follows: 1) The growth rate, the consumption and efficiency ratios of the food and protein in each experimental diet group added ginseng steamed leaf or trunk were higher than those in experimental group A which has the diet supplemented with ginseng raw leaf of trunk. 2) The absorption rates of the carbohydrate were above 96%, higher than those or the control group, But those of fat, protein and the utilization rate of energy in each experimental diet group were generally lower than those in the control group.

• 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.

• Journal of Nutrition and Health
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• v.30 no.6
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• pp.605-613
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• 1997

This study was to investigate interaction between dietary protein and Ca levels in Ca metabolism and renal function in osteporosis rats. Five week-old female rats were fed a low Ca diet for 4 weeks after ovariectomy operation to establish rat models of osteoporosis. The ovariectomized osteoporosis rats were divided into six groups and were fed experimental diets which contained two levels of protein, normal (20%) and high(40%) , and three levels of Ca, low (0.06%), normal (0.47%) and high(0.94%) for 4 weeks , respectively. The ovaricetmized rat model of osteoporosis showed a remarkable decrease in serum Ca concentration, fresh weight and breaking force of femur, Ca and P contents of femur, and apparent absorption and retention of Ca. The supplementations of Ca and P contents of femur, and apparent absorption and retention of Ca. The supplementations of Ca at the dietary levels of normal and high levels significantly enhanced Ca bioavailability shown in the above experimental rat models of osteoporosis, regardless of dietary protein levels ; whereas the rats which were fed the low Ca diet demonstrated rather a decrease in its bioavailability. Irrespectively of the dietary Ca levels, the rats which were fed high protein diet exhibited an increase in kidney weight, urinary Ca, volume and hydroxyproline, and glomerular filtration ratio(GFR). The results show that dietary protein and calcium levels affect the renal function and Ca metabolism independently, while the interaction between protein and calcium have not been shown.

• Rapid Communication in Photoscience
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• v.4 no.1
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• pp.1-8
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• 2015

For understanding molecular mechanisms of photochemical reactions, in particular reactions of proteins with biological functions, it is important to elucidate both the initial reactions from the photoexcited states and the series of subsequent chemical reactions, e.g., conformation, intermolecular interactions (hydrogen bonding, hydrophobic interactions), and inter-protein interactions (oligomer formation, dissociation reactions). Although time-resolved detection of such dynamics is essential, these dynamics have been very difficult to track by traditional spectroscopic techniques. Here, relatively new approaches for probing the dynamics of protein photochemical reactions using time-resolved transient grating (TG) are reviewed. By using this method, a variety of spectrally silent dynamics can be detected and such data provide a valuable description about the reaction scheme. Herein, a blue light sensor protein TePixD is the exemplar. The initial photochemistry for TePixD occurs around the chromophore and is detected readily by light absorption, but subsequent reactions are spectrally silent. The TG experiments revealed conformational changes and changes in inter-protein interactions, which are essential for TePixD function. The TG experiments also showed the importance of fluctuations of the intermediates as the driving force of the reaction. This technique is complementary to optical absorption detection methods. The TG signal contains a variety of unique information, which is difficult to obtain by other methods. The advantages and methods for signal analyses are described in detail in this review.

• 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 Life Science
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• v.19 no.11
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• pp.1591-1597
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• 2009

The aim of this study was to examine the effects of Capsosiphon fulvescens extract (CFE) on levels of essential amino acids in serum and the rate of protein digestion. CFE contains approximately 68% carbohydrate as fiber, 17% crude ash, and 14% crude protein. Experimental rats were divided two groups, one group receiving a normal diet and the other a normal diet containing 5% CFE. To analyze the absorption of essential amino acids into the hepatic portal vein, blood from the hepatic portal vein was collected between 10 a.m. and 5 p.m. for 10 days. In vitro protein digestion was decreased in the group fed 5% CFE; these data indicated that CFE affected protease activity. We measured the absorption of essential amino acids in the serum of the hepatic portal vein, at 30-, 60-, 90-, and 120 minutes after feeding. Although there was no difference in the concentration of total essential amino acids between the two groups, the 5% CFE-fed animals had a decreased rate of absorption. Absorption of Lys and Thr into the hepatic portal vein was lower in the CFE-fed group than in the control group. The rate of absorption of Met was delayed nearly 50% in the CFE-fed group compared to the control group. On the other hand, the rate of absorption of Leu, Ile, and Val was increased; Phe showed the same. Therefore, we suggest that CFE could affect protein metabolism by increasing or decreasing the absorption rate of essential amino acids.

• Korean Journal of Food Science and Technology
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• v.30 no.3
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• pp.557-561
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• 1998

This study was conducted to investigate the functionality of soybean protein isolates extracted in acidic range (pH 2.0 and 3.0), neutral range (pH 7.0) and alkaline range (pH 10.0 and 12.0). The protein content of soybean protein isolates extracted at pH 3.0 was maximum (93.31%), but that of pH 7.0 was minimum (73.93%). The extraction yield of soybean protein isolates extracted at pH 3.0 was minimum (0.36%), but that of pH 12.0 was maximum (47.54%). The functionality (solubility, water absorption, oil absorption, foam capacity, foam stability, emulsion capacity and gelation) of soybean protein isolates was significantly influenced by pH of extraction medium. The soybean protein isolates extracted at pH 2.0 and 3.0 were more soluble at acidic ranges and those of pH 3.0 and 7.0 were more soluble at neutral ranges, but those of pH 2.0, 3.0, 7.0, 10.0 and 12.0 were more soluble at alkaline ranges than other ranges. The soybean protein isolates extracted at pH 2.0 and pH 12.0 gave greater water absorption, oil absorption and foam capacity than those extracted at pH 3.0, pH 7.0 and pH 10.0. And the emulsion capacity of soybean protein isolates was increased by the increase of extraction pH.