• Preventive Nutrition and Food Science
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• v.11 no.1
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• pp.73-77
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• 2006

Ground pork was irradiated with an electron beam (e-beam) at a dose of 0, 1.5, 3, 5 and 10 kGy and the changes in various functional and other associated properties of salt-soluble proteins extracted from the pork were evaluated. Irradiation did not affect turbidity and the disulfide content of pork salt-soluble protein, but the content of sulfhydryls and the hydrophobocity of salt-soluble protein increased. This indicates that protein degradation occurred when the pork was e-beam irradiated and that the sulfhydryls and hydrophobic moieties buried inside the proteins were exposed to the outside environment. However, these degraded protein molecules did not form large protein aggregates through disulfide bridges. The emulsifying capacity of the pork increased with irradiation, which could be the result from increased hydrophobicity of pork salt-soluble protein. Water holding capacity of pork was not affected bye-beam irradiation.

• Journal of Animal Science and Technology
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• v.62 no.4
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• pp.533-542
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• 2020

The objective of this study was to observe the interactions between salt-soluble proteins extracted from beef and elephant foot yam (Amorphophallus campanulatus) flour in heat-induced gel matrix development. The effect of salt concentration; 0.5%, 1.0%, 1.5%, and 2.0% in weight/weight basis (w/w), during protein extraction on pH, salt-soluble protein concentration and myofibril fractions of beef extract was determined firstly, and no significant effect was found. The beef salt-soluble proteins extracted using salt solution at different concentrations were then added with elephant foot yam flour at 5%, 10%, and 15% w/w, gelatinized at 90℃ for 20 min, and cooled down at 4℃ for 12 h. The interactions between beef salt-soluble proteins and elephant foot yam flour resulted in an improved gel strength (p < 0.01) and the addition level of elephant foot yam flour affected the pH, instrumental color, moisture, crude protein, and ash content significantly. The addition of elephant foot yam flour also reduced the size of the pores in the gel matrix as shown by scanning electron microscope (SEM) photographs. These suggest that elephant foot yam flour well interacts with beef salt-soluble proteins to form gel matrix.

• Food Science of Animal Resources
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• v.18 no.3
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• pp.209-215
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• 1998

Effects of protein concentration, ionic strength, pH, and temperature range on the heat-induced denaturation of salt soluble protein extracted from spent layer meat were investigated. Viscosity of salt soluble protein heated at 65$^{\circ}C$ for 30 min began to increase sharply above 7 mg/ml of breast protein concentration, and above 21 mg/ml of leg protein concentration, respectively. Both turbidity and viscosity showed the highest value in cooked protein solution with pH 6.0 and 1% NaCl. The turbidity of salt soluble protein started to increase continuously from 40$^{\circ}C$ to 80$^{\circ}C$. The viscosity increased rapidly from 45$^{\circ}C$ to 60$^{\circ}C$ in breast protein, and increased from 50$^{\circ}C$ to 55$^{\circ}C$ in leg protein, respectively, and then kept relatively constant. Breast protein had higher viscosity than leg protein during heat-induced gelation. Therefore, salt soluble protein from spent layer meat was associated with denatured protein (turbidity change) prior to gelation (viscosity change) during heating. Breast protein showed lower thermal transition temperature, and better gel formation than leg protein during heating.

• Food Science of Animal Resources
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• v.43 no.6
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• pp.1031-1043
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• 2023

The purpose of this study was to investigate the functional properties of salt-soluble proteins obtained from Protaetia brevitarsis (PB) and Tenebrio molitor (TM) larvae, the interaction between these proteins and pork myofibrillar protein (MP) in a gel system. The gel properties of salt-soluble protein extracts showed that the PB had a higher viscosity than the TM protein. However, the TM protein had higher gel strength compared with the PB protein. The gelation characteristics of the pork MP gel systems added with lyophilized insect salt-soluble protein powder showed to decrease slightly viscosity compared with MP alone. Adding the TM or PB protein powder did not affect the pork MP's hydrophobicity and sulfhydryl group levels. Furthermore, the protein bands of the MP did not change with the type or amount of insect salt-soluble protein. The cooking yields of the pork MP gels containing PB or TM protein powder were higher than those without insect protein. Regardless of the type of insect salt-soluble protein added, the pork MP's gel strength decreased. Furthermore, as the level of insect powder increased, the surface protein structure became rough and porous. The results demonstrated that proteins extracted from PB and TM larvae interfered with the gelation of pork MP in a gel system.

• Korean journal of food and cookery science
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• v.17 no.5
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• pp.503-509
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• 2001

The effects of salting methods on textural properties of Kakdugi were evaluated during fermentation at 1$0^{\circ}C$ for up to 52 days. Kakdugi samples were prepared by 4 different salting methods at final salt concentration of 1.5%, which is appropriate for organoleptic quality. The salting methods for radish cubes(2 cm size) of Kakdugi were as follows; 1) Treatment S-1: spraying dry salt uniformly on to the radish cubes at 1.5%(w/w) and holding for 1 hr, 2) Treatment S-5: spraying dry salt uniformly on to the radish cubes at 1.2%(w/w) and holding for 5 hr, 3) Treatment B-1: brining radish cubes in a 8.5%(w/v) salt solution for 1 hr, 4) Treatment B-5: brining radish cubes in a 4.0%(w/v) salt solution for 5 hr. The contents of water soluble pectin, total soluble solid and PG activity were increased as the fermentation periods increased. A majority of total dietary fiber(TDF) consisted of soluble dietary fiber(SDF), and the amount of insoluble dietary fiber(IDF) was relatively small in Kakdugi during fermentation. Furthermore, an increase in SDF and a consequent decrease in IDF contents were observed with the fermentation time increased.

• Preventive Nutrition and Food Science
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• v.10 no.4
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• pp.378-381
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• 2005

Actin and myosin solutions and fresh ground pork were irradiated with the electron beam (e-beam) at a dose of 0, 1.5, 3.0, 5.0 and 10 kGy. The changes in SDS-PAGE pattern of 2 proteins and the salt-soluble proteins extracted from ground pork after e-beam irradiation were monitored. When the myosin solution was irradiated with e-beam, myosin was degraded completely. Complete myosin degradations were observed even with the lowest dose (1.5 kGy) of e-beam treatment. Actin was degraded with the irradiation, but to a less extent than myosin was. The degradation of actin increased as the e-beam treatment increased from 1.5 to 10.0 kGy. Among the salt-soluble proteins extracted from ground pork, myosin was degraded gradually when the e-beam dose increased from 1.5 up to 10.0 kGy. Similar gradual increase in the degradation of actin also occurred with the increase of irradiation. Increases of 2 low molecular weight compounds (<29 kDa) were observed when the irradiation dose increased from 1.5 to 10.0 kGy. These 2 molecules are thought to be the breakdown products produced from the degradation of major salt-soluble proteins, myosin and actin. The salt-soluble protein content of ground pork did not change with the e-beam irradiation.

• Applied Biological Chemistry
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• v.36 no.3
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• pp.172-177
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• 1993

To extract insoluble proteins from sesame meal residue by microorganism, the sesame meal residue was treated with crude enzyme solution of Bacillus sp. CW-1121. The foaming capacity of salt soluble protein was quite lower than that of water soluble protein and the foaming stability of salt soluble protein decreased abruptly in 10 min., while it sustained for 30 min in case of water soluble protein. Emulsion capacities of all the protein fractions showed minimum value near isoelectric point of protein and salt soluble protein had lower emulsion capacities than that of water soluble protein. The emulsion stability of the protein was relatively stable for 30 min at $80^{\circ}C$. Oil and water absorption capacities of salt soluble protein were higher than those of water soluble protein.

• Journal of architectural history
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• v.22 no.6
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• pp.59-66
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• 2013

This study progressed an investigation on the cause of the efflorescence phenomenon of bricks in Suwon Hwaseong Fortress, which is designated as a UNESCO World Heritage by using diverse scientific analyses. The samples were taken in Hwaseong and analyzed using XRD and SEM-EDS for the material identification of efflorescence. We observed under a polarizing microscope and measured absorption factors for the basic investigation for traditional bricks. As a result of material identification, soluble salt($Na_2SO_4$, $KNO_3$) and insoluble salt($CaCO_3$) were detected. There was no big difference between original bricks and repaired bricks under the polarizing microscope. However, in terms of the water absorption rate, bricks which were used for repair nowadays showed low water absorption rate(1%). In conclusion, soluble salt and insoluble salt appeared due to an effect of an air pollution and joint mortar. Soluble salt was removed in the rainy season, but insoluble salt was not removed. As a result of the efficiency and safety tests for chemicals removing efflorescence, chemical E is likely to be the suitable chemicals for the efflorescence phenomenon of traditional bricks in Suwon Hwaseong Fortress. In the future, consideration whether the use of lime is available or not should be studied through comprehensive researches including repair work, construction work and the environment factor with lime. Also, physical, chemical identifications of repairing bricks will be required.

• Korean Journal of Food Science and Technology
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• v.30 no.6
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• pp.1388-1393
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• 1998

Traditional Andong sikhe was produced by fermenting L. bulgaricus LBS 47 and S. cerevisiae SCS 5. The changes of nitrogen compound and amino acid during fermentation and storage were investigated. Crude protein was increased until 4days, the main fermentation period. Amino form nitrogen increased up to 37.50 mg% at the 2nd day of fermentation and the product tasted best at this time. Water soluble and salt soluble protein decreased during fermentation. Proline and aspartic acid were the two major free amino acids. The free methionine increased while the free lysine decreased in the process of fermentation. The amino acids of water soluble protein and salt soluble protin were totally 17 kinds. The major amino acids of water soluble and salt soluble protein were glutamic acid and aspartic acid. The arginine content of salt soluble protein increased as the fermentation proceeded.

• Food Science of Animal Resources
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• v.39 no.4
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• pp.643-654
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• 2019

The amino acid composition, protein quality, and protein functionality of protein solution extracted from three edible insect species were investigated. We used 0.02% ascorbic acid and 0.58 M saline solution to extract water-soluble and salt-soluble proteins from the three insect species. Extracted protein solutions of Tenebrio molitor (TM), Allomyrina dichotoma (AD), and Protaetia brevitarsis seulensis (PB) were divided into six groups, according to species and solubility: WTM, WAD, WPB (water-soluble), and STM, SAD, and SPB (salt-soluble). Defatted TM had the highest protein content, but its protein solubility was the lowest, for both water and saline solutions. Amino acid composition differed by edible insect species and buffer type; SPB had the highest protein quality, followed by WPB. PB had a higher pH than the other species. Color values also differed among species. SPB had abundant high molecular weight proteins, compared with other treatments; and also had the highest foaming capacity, foam stability, and emulsifying capacity. In conclusion, PB is a good source of functional protein compared with the other studied species. Additionally, protein extraction using saline solution is promising as a useful method for improving edible insect protein functionality.