• IMMUNE NETWORK
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• v.9 no.6
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• pp.265-273
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• 2009

Foot-and-mouth disease virus (FMDV) is a small single-stranded RNA virus which belongs to the family Picornaviridae, genus Apthovirus. It is a principal cause of FMD which is highly contagious in livestock. In a wild type virus infection, infected animals usually elicit antibodies against structural and non-structural protein of FMDV. A structural protein, VP1, is involved in neutralization of virus particle, and has both B and T cell epitopes. A RNA-dependent RNA polymerase, 3D, is highly conserved among other serotypes and strongly immunogenic, therefore, we selected VP1 and 3D as vaccine targets. VP1 and 3D genes were codon-optimized to enhance protein expression level and cloned into mammalian expression vector. To produce recombinant protein, VP1 and 3D genes were also cloned into pET vector. The VP1 and 3D DNA or proteins were co-immunized into 5 weeks old BALB/C mice. Antigen-specific serum antibody (Ab) responses were detected by Ab ELISA. Cellular immune response against VP1 and 3D was confirmed by ELISpot assay. The results showed that all DNA- and protein-immunized groups induced cellular immune responses, suggesting that both DNA and recombinant protein vaccine administration efficiently induced Ag-specific humoral and cellular immune responses.

• BMB Reports
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• v.31 no.3
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• pp.221-226
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• 1998

Phosphorylation of phytochrome may play important functional roles to control plant photomorphogenesis. Many attempts have failed to identify the protein kinase that phosphorylates phytochrome in vivo. It has been reported that a polycation-stimulated protein kinase activity was associated with the purified phytochrome. However, it is not known if the kinase activity is an intrinsic property of phytochrome or whether it comes from a contaminant of the purified phytochrome. In the present study, three protein kinases that phosphorylate phytochrome have been identified from etiolated oat seedlings. A polycationstimulated protein kinase that had very similar enzymatic properties with that associated with the purified phytochrome was identified in the cytosolic extract. It phosphorylated several contaminant proteins in the kinase preparation as well as phytochrome and had a broad substrate specificity. A CK II-type protein kinase phosphorylated phytochrome and the exogenously added casein. It is likely that this kinase may not be a feasible candidate for the kinase phosphorylating phytochrome in vivo since the content of the kinase seemed to well exceed the content of phytochrome in the etiolated oat seedlings. Another protein kinase that had unique enzymatic properties phosphorylated phytochrome very specifically and seemed to be present in a small quantity in the etiohlted seedlings. It is expected that one of three kinases may be responsible for the phytochrome phosphorylation in vivo.

• Asian-Australasian Journal of Animal Sciences
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• v.23 no.5
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• pp.598-606
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• 2010

This study investigated the nutritional quality of soybean meal (SBM) fermented by Aspergillus ($FSBM_A$) and/or followed by Lactobacillus fermentation ($FSBM_{A+L}$). Both fermented products significantly improved protein utilization of SBM with higher trichloroacetic acid (TCA) soluble true protein content, in vitro protein digestibility and available lysine content, especially in $FSBM_{A+L}$. Moreover, $FSBM_{A+L}$ produced a huge amount of lactic acid resulting in lower pH as compared to the unfermented SBM or soybean protein concentrate (SPC) (p<0.05). $FSBM_A$ and $FSBM_{A+L}$ raised 4.14% and 9.04% of essential amino acids and 5.38% and 9.37% of non-essential amino acids content, respectively. The ${\alpha}$-galactoside linkage oligosaccharides such as raffinose and stachyose content in $FSBM_A$ and $FSBM_{A+L}$ decreased significantly. The results of soluble protein fractions and distribution showed that the ratio of small protein fractions (<16 kDa) were 42.6% and 63.5% for $FSBM_A$ and $FSBM_{A+L}$, respectively, as compared to 7.2% for SBM, where the ratio of large size fractions (>55 kDa, mainly ${\beta}$-conglycinin) decreased to 9.4%, 5.4% and increased to 38.8%, respectively. There were no significant differences in ileal protein digestibility regardless of treatment groups. SPC inclusion in the diet showed a better protein digestibility than the SBM diet. In summary, soybean meal fermented by Aspergillus, especially through the consequent Lactobacillus fermentation, could increase the nutritional value as compared with unfermented SBM and is compatible with SPC.

• Food Science of Animal Resources
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• v.42 no.3
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• pp.536-555
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• 2022

The most abundant Orthoptera in Mexico is a small grasshopper (Sphenarium purpurascens) which is considered a food source with increased nutritional value due to its high protein content. Insect proteins have gained relevance because of their high potential as gelling, texturing, and extender agents in the food industry. The objective of this study was to evaluate the effect of substituting meat with a soluble protein extract from grasshopper obtained by alkalisation or alkalisation-piezoelectric ultrasound, on the techno-functional, physicochemical, and sensory characteristics of cooked meat models (sausages). The soluble protein was extracted in NaHCO₃ pH 8 and a piezoelectric ultrasound 5-mm sonotrode at 20 kHz with 99% amplitude. Different formulations with meat substitution: 0%, 5%, 10%, and 15% were prepared and characterised for their rheological behaviour, emulsion stability, weight loss by cooking, total protein content, colour, and texture. Sensory evaluation was conducted with consumers using a test involving check-all-that-apply and overall liking. The alkalisation-piezoelectric ultrasound method improved the solubility and the techno-functional properties of the soluble grasshopper protein when applied in sausages at maximum levels of 10% meat substitution. The sensory evaluation indicated that the formulation with 5% meat substitution exhibited the same acceptability as the control sample. Given these results, the soluble protein treated with alkalisation and piezoelectric ultrasound could be used as an extender in meat products.

• Journal of Veterinary Science
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• v.21 no.2
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• pp.33.1-33.15
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• 2020

Bovine ephemeral fever virus (BEFV) causes bovine ephemeral fever, which can produce considerable economic damage to the cattle industry. However, there is limited experimental evidence regarding the underlying mechanisms of BEFV. Annexin A2 (AnxA2) is a calcium and lipid-conjugated protein that binds phospholipids and the cytoskeleton in a Ca²⁺-dependent manner, and it participates in various cellular functions, including vesicular trafficking, organization of membrane domains, and virus proliferation. The role of the AnxA2 gene during virus infection has not yet been reported. In this study, we observed that AnxA2 gene expression was up-regulated in BHK-21 cells infected with the virus. Additionally, overexpression of the AnxA2 gene promoted the release of mature virus particles, whereas BEFV replication was remarkably inhibited after reducing AnxA2 gene expression by using the small interfering RNA (siRNA). For viral proteins, overexpression of the Matrix (M) gene promotes the release of mature virus particles. Moreover, the AnxA2 protein interaction with the M protein of BEFV was confirmed by GST pull-down and co-immunoprecipitation assays. Experimental results indicate that the C-terminal domain (268-334 aa) of AxnA2 contributes to this interaction. An additional mechanistic study showed that AnxA2 protein interacts with M protein and mediates the localization of the M protein at the plasma membrane. Furthermore, the absence of the AnxA2-V domain could attenuate the effect of AnxA2 on BEFV replication. These findings can contribute to elucidating the regulation of BEFV replication and may have implications for antiviral strategy development.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.35 no.5
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• pp.464-475
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• 1990

To obtain the basic informations about the repeseed Quality improvement, If varieties were analyzed for their seed protein content and amino acid composition, and discussed comparing to several other oilseed crops or varietal origin and seed weight or maturity. Total protein content of the tested varieties were ranged from 15.3 to 36.2% with mean protein content of 23.2%. The highest protein content was recorded in B. hirta var. Ochre, whereas the lowest in B. napus var. Mirado. Grouped by seed weight, small seed varieties were higher in protein content. A high negative correlation (-0.524) was observed between the content of protein and oil. Further, more the relationship between protein content and 1,000 seed weight was also very significant with the correlation coefficient of -0.622. The amino acid composition of rapeseed meal was characterized by a relatively high methionine and lysine content. Main amino acids were glutamic and aspartic acid in rapeseed.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.34 no.1
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• pp.21-26
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• 2001

To examine functionality of depolymerized alginate obtained by hydrolysis of alginate through a heating process at $121^{\circ}C$ on gastrointestinal physiology, the changes of body weight, organ weight and length, pancreatic and small intestinal composition, and light microscopy (LM) observation of small intestinal microvilli's appearances were checked in the rats. Rats were fed diets containing $1\%, 5\%, and 10\%$ of each depolymerized alginate (HAG-10, HAG-50, HAG-100) and alginate for 35 days, The feeding of 5 and $10\%$ HAG-50 and $10\%$ alginate diets for 35 days significantly depressed the body weight gain, but increased the length and weight of the small intestine and cecum in rats (p<0.01). Pancreatic protease activity was decreased significantly (p<0.01) in all groups except lo/o of HAG-10 diets, but the protein content increased in all groups, However, pancreatic amylase and lipase activities as well as DNA and RNA content were not significantly different. The small intestinal protein and the DNA content were the highest in diets fed $5\%$ HAG-50; RNA content increased significantly (p<0.01) in all groups except in the fiber-free diets. Light microscopy (LM) observation showed growth of small intestinal microvilli with numerous ridges; the multiplication of the convolution goblet cells in rats fed with diets containing $5\%$ of HAG-50 were more than others group.

• Journal of Aquaculture
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• v.7 no.3
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• pp.165-175
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• 1994

Attempts were made to find out nitrogen and phosphorus loads to aquatic environment resulting from feeding Nile tilapia (Oreochromis niloticus). Two different size groups, small and large, were used. The average sizes of small and large tilapia were 65.2 g and 389.2 g respectively, and three kinds of commercial diets were used for each size. The 3 kinds of commercial diets for tilapia contained in average 33.8% crude protein ($5.4\%$ nitrogen) and $1.4\%$ total phosphorus. The load of nitrogen and phosphorus were measured by subtracting the amounts of nutrients retained in the body of fish from consumed nutrients. Sixty, five percentage of total feces was excreted within 24 hours after feeding at $23^{\circ}C$. Nitrogen content in the feces was higher in large fish than small ones. The apparent digestibility of dietary protein for small and large tilapia was $90.0\%$ and $89.7\%$, respectively. Availability of dietary phosphorus for small and large tilapia was $44.7\%\;and\;51.4\%$, respectively. The total load of nitrogen and phosphorus per 1 metric ton of tilapia production was 49.5kg and 6.3kg, respectively, for small ones with feed conversion ratio (FCR) of 1.4, and 61.3 kg and 13.4kg, respectively, for large ones with the FCR of 1.8. Nitorgen balance appeared that small and large tilapia excreted $7.1\%\;and\;9.9\%$ of consumed nitrogen through fecal-nitrogen and $55.5\%\;and\;62.3\%$ through urine and gills, retaining $37.4\%\;and\;27.8\%$ in the body, respectively. These results show that small fish pollute less than large fish, excreting less and retaining more nutrients in the body.

• Korean Journal of Food Science and Technology
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• v.26 no.2
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• pp.110-116
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• 1994

In order to study the effects of enzyme modification on the physico-chemical and functional properties of myofibrillar protein prepared from the frozen sardine, Sardinops melanostica, the protein was hydrolyzed with pepsin under the enzyme-substrate ratio 1:100 at $37^{\circ}C$ and pH 1.65 for 1, 4, 8, 12, and 24 hr, respectively. The properties of pepsin-modified sardine myofibriliar protein were determined. The extents of proteolysis with pepsin as a fuction of time was showed a typical enzyme hydorlysis curve with an initial region of 4 hour period followed by plateau region. The SDS-acrylamide slab gel electrophoresis patterns of pepsin-modified proteins showed mainly disappearances of minor protein bands, but no changes of main protein bands. The gel filtration patterns through Sephadex G-75 of sardine myofibrillar protein showed two big peaks and three small peaks. All the small peaks were disappearanced by proteolysis with pepsin in one hour. and during the period of proteolysis the fast big peak became gradually smaller and the late big peak eluted more slowly. By proteolysis, the emulsifying activity and emulsifying capacity of sardine myofibrillar protein were all decreased. The effects of pepsin-modification on emulsifying capacity were greater than those on emulsifying activity of protein. The aeration capacity of the protein was increased about 1.9 folds and the foam stability decreased to 0.6 folds of control by pepsin-modification. The pepsin-modified sardine myofibrillar proteins showed about 0.6 folds of heat coagulation and 1.4 folds of viscosity of control. The pH dependence of solubilities of sardine myofibrillar protein showed two isoelectric areas of pH 5 and 9. The pepsin-modified protein showed more clear pH dependences at the early stage but not at the late stage of proteolysis.

• Proceedings of the Zoological Society Korea Conference
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• 2001.10a
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• pp.192.2-192
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• 2001

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