• Journal of the Korean Society of Food Culture
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• v.14 no.5
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• pp.477-485
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• 1999

This study was conducted to improve the functional properties of soybean protein isolate by dimethylglutarylation and acetylation. Amino acid composition and solubility of modified soybean protein by dimethylglutarylation were not changed, but lysine and trypsin inhibitor activity was decreased an isoelectric point was moved from pH5 to pH4 as a result of modification. Emulsification capacity and stability, foaming capacity and thermal stability were increased by the modification. In that 91% dimethylglutarylated protein did not coagulate when heating at $100^{\circ}C$ for 20 min. while its foaming stability was decreased. Whereas specific gravity was decreased by the modification of the soybean protein, relative viscosity and whiteness were improved. Generally, dimethylglutarylation produced more conformational changes in protein system than did in acetylation.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.8
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• pp.1158-1164
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• 2003

In two feeding experiments male and mixed-sex broiler chicks were offered diets based on sorghum and a wheatsorghum blend with two tiers of nutrient specifications, without and with microbial phytase (600 and 800 FTU/kg), from 7-25 and 1-42 days post-hatch, respectively. The nutrient specifications for protein, amino acids, energy density and phosphorus (P) of standard diets were reduced to formulate the modified diets on a least-cost basis. Calculated differences in nutrient specifications between standard and modified diets ranged from 14.3 to 17.1 g/kg crude protein, 0.24 to 0.40 MJ/kg apparent metabolisable energy (AME) and 1.06 to 1.20 g/kg available P. In both experiments, reduced nutrient specifications had a negative impact on growth rates and feed efficiency and phytase supplementation had a positive influence on growth performance and protein efficiency ratios (PER). Phytase addition to the less expensive, modified diets either partially or entirely compensated for reduced growth performance and, consequently, feed costs per kg of live weight gain were reduced. In Experiment 1, phytase increased (p<0.001) nitrogen-corrected AME (AMEn) from 15.39 to 15.89 MJ/kg dry matter. For nitrogen (N) retention there was an interaction (p<0.05) between diet type and phytase as the effects of phytase on N retention were more pronounced in the modified diets, with an increase from 0.512 to 0.561. These results demonstrate the positive effects of phytase on protein and energy utilisation, in addition to its established liberation of phytate-bound P and illustrate the feasibility of assigning nutrient replacement values to the feed enzyme for consideration in least-cost ration formulations. Further work is, however, required to define the most appropriate reductions in nutrient specifications in association with phytase supplementation.

• Korean Journal of Agricultural Science
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• v.45 no.2
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• pp.248-257
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• 2018

Overexpression of AtCYP78A7, a gene encoding a cytochrome P450 protein, has been reported to improve tolerance to drought stress in genetically modified (GM) rice (Oryza sativa L.). The aim of this study was to evaluate the potential allergenicity and acute oral toxicity of the AtCYP78A7 protein expressed in GM rice. Bioinformatics analysis of the amino acid sequence of AtCYP78A7 did not identify any similarities with any known allergens or toxins. It showed that no known allergen had more than a 35% amino acid sequence homology with the AtCYP78A7 protein over an 80 amino acid window or more than 8 consecutive identical amino acids. The gene encoding the AtCYP78A7 protein was cloned in the pGEX-4T-1 vector and expressed in E. coli. Then, the AtCYP78A7 protein was purified and analyzed for acute oral toxicity. The AtCYP78A7 protein was fed at a dose of 2,000 mg/kg body weight in mice, and the changes in mortalities, clinical findings, and body weight were monitored for 14 days after the dosing. Necropsy was carried out on day 14. The protein did not cause any adverse effects when it was orally administered to mice at 2000 mg/kg body weight. These results indicate that the AtCYP78A7 protein expressed in GM rice would not be a potential allergen or toxin.

• BMB Reports
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• v.41 no.3
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• pp.194-203
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• 2008

Nitrosative modifications regulate cellular signal transduction and pathogenesis of inflammatory responses and neuro-degenerative diseases. Protein tyrosine nitration is a biomarker of oxidative stress and also influences protein structure and function. Recent advances in mass spectrometry have made it possible to identify modified proteins and specific modified amino acid residues. For analysis of nitrated peptides with low yields or only a subset of peptides, affinity 'tags' can be bait for 'fishing out' target analytes from complex mixtures. These tagged peptides are then extracted to a solid phase, followed by mass analysis. In this review, we focus on protein tyrosine modifications caused by nitrosative stresses and proteomic methods for selective enrichment and identification of nitrosative protein modifications.

• Journal of the Korean Home Economics Association
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• v.28 no.4
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• pp.41-50
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• 1990

Soy protein was isolated from Korean soy bean 'Chang ryub' and chemically modified with succinic anhydride. Functionality of the soy protein isolate(SPI), succinylated SPI(SPPI), and PP590(commercial) at various pH were investigated. The mechanical and sensory properties of soy bean curds made from several mixing ratio of succinylated soy bean milk were observed. The solubility of SPI significantly increased with succinylation. The solubility of PP590 was lower than that of SSPI. The solubility of SPPI increased significantly in 0.03M CaCl2 solution. The emulsifying activity of SSPI increased. On the range of pH above pI the emulsifying activity of PP590 was higher than that of SPI. There was no difference in emulsion stability among the groups. The foam expansion capacity of SPPI increased at higher pH than pI but the foam stability decreased significantly above pH 9. Mechanical texture profile analysis revealed the modified soy bean curds had the lower hardniss, chewiness and cohesiveness with increased modification. The mechanical characteristics of modified soy bean curds revealed generalized Maxwell Model of 7-elements or 5-elements. In sensory evaluation, the hardness, the springiness and acceptability of modified soy bean curds were lower significantly than those of control soy bean curd.

• Korean Journal of Food Science and Technology
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• v.24 no.3
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• pp.294-299
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• 1992

This study was to examine the effect of functional properties of soy protein isolate(SPI) and qualities of soybean curd upon proteolytic hydrolysis. SPI was hydrolyzed using proteolytic enzyme, bromelain. The protein content of SPI by microkjeldahl method was 84% and the degree of hydrolysis in modified soy protein isolate(MSPI) was 2.7%. The solubility of MSPI was higher than that of control at various pH tested and proteolytic hydrolysis was increased emulsion formation and foam expansion while decreased emulsion stability, foam stability and calcium precipitation. Modified soybean curdI, standard soybean milk: Modified soybean milk=3:1, was soft and springy soybean curd when the texture properties of soybean curd were tested by texture profile analysis using Instron and sensory evaluation. The rheological model of soybean curds was investigated by stress relaxation test. The analysis of relaxation curve revealed that the rheological behavior of soybean curds could be expressed by 7-element generalized Maxwell model. The equilibrium modulus and modulus of elasticity decreased as the ratio of modified soybean milk was increased.

• Journal of Microbiology and Biotechnology
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• v.12 no.2
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• pp.306-311
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• 2002

O-linked N-acetylglucosamine (O-GlcNAc) is an abundant posttranslationally modified compound in eukaryotic cells. Human O-GlcNAc transferase (OGT) was produced as a maltose binding protein (MBP) fusion protein, which showed significant catalytic activity to modify recombinant Sp1, transcription factor. To facilitate the production of O-GlcNAc modified proteins, instead of using the tedious in vitro glycosylation reaction or expression in eukaryotic cells, a MBP-fusion OGT expression vector (pACYC184-MBPOGT) was constructed using pACYC184 plasmid, which could coexist with general prokaryotic expression vectors containing ColE1 origin. By cotransforming pACYC184-MBPOGT and pGEX-2T vectors into Escherichia coli BL21, intracellular O- GlcNAcylated proteins could be obtained by a simple purification procedure. It is expected that this may be a useful tool for production of O-GlcNAc modified proteins.

• Food Science and Biotechnology
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• v.18 no.1
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• pp.60-65
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• 2009

Near infrared reflectance spectroscopy (NIRS) was used as a rapid and non-destructive method to determine the protein content in intact and ground seeds of pea (Pisum sativum L.) germplasms grown in Korea. A total of 115 samples were scanned in the reflectance mode of a scanning monochromator at intact seed and flour condition, and the reference values for the protein content was measured by auto-Kjeldahl system. In the developed ground and intact NIRS equations for analysis of protein, the most accurate equation were obtained at 2, 8, 6, 1 math treatment conditions with standard normal variate and detrend scatter correction method and entire spectrum (400-2,500 nm) by using modified partial least squares regression (n=78). External validation (n=34) of these NIRS equations showed significant correlation between reference values and NIRS estimated values based on the standard error of prediction (SEP), $R^2$, and the ratio of standard deviation of reference data to SEP. Therefore, these ground and intact NIRS equations can be applicable and reliable for determination of protein content in pea seeds, and non-destructive NIRS method could be used as a mass analysis technique for selection of high protein pea in breeding program and for quality control in food industry.

• Korean Journal of Food Science and Technology
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• v.20 no.5
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• pp.625-630
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• 1988

Phosphorylation of soy protein by sodium trimetaphosphate and acetylation of soy protein by acetic anhydride were performed. Then, the functional properties of modified soy proteins were compared with that of unmodified soy protein. Isolated soy protein prepared from defatted soybean flake had protein content of 92.7% as moisture-free basis. The phosphorylated soy protein showed higher solubility, foaming properties, and water holding capacity than unmodified soy protein. Acetylation of soy protein increased emulsification activity and foaming properties greatly, whereas decreased the solubility at pH 8.0. Isoelectric pHs of phosphorylated and acetylated soy protein were shifted to acidic regions(pH 3.0 and pH 4.0) from pH 5.0, which was the isoelectric pH of unmodified soy protein. Soy protein seems to be aggregated during phosphorylation and acetylation procedure, judging form Sepharose CL-4B gel filtration profiles. The modified soy proteins showed increased mobilities to anode direction in disc-gel electrophoresis.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.3
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• pp.219-223
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• 1990

Myofibrillar protein from Alaska pollack was modified with acetic anhydride at pH 7.5 and $25^{\circ}C$ and changes in functional properties as affected by the degree of modification were determined. Acetylation of myofibrillar protein resulted in protein with unique functional properties dependent upon the degree of acetylation. By selecting appropriate degree of modification it was possible to control protein solubility heat coagulability calcium precipitability foaming and emulsion capa-city.