• Bulletin of the Korean Chemical Society
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• v.33 no.10
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• pp.3378-3382
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• 2012

A superhydrophobic surface with a water contact angle > $150^{\circ}$ has attracted great interest from both fundamental and practical aspects. In this study, we demonstrated that hydrophobicity of a silica nanotube (SNT) array can be easily controlled by the SNT aspect ratio. In addition, the adhesive and anti-adhesive properties were controlled without modifying the hydrophobic surface. Various silica structures on a polydimethylsiloxane substrate were prepared using the desired alumina template. Bundle-arrayed and bowl-arrayed silica surfaces exhibited extraordinary superhydrophobicity due to the large frontal surface area and hierarchical micro/nanostructure. As the strategy used in this study is biocompatible and a wide range of hydrophobicities are capable of being controlled by the SNT aspect ratio, a hydrophobic surface composed of an SNT array could be an attractive candidate for bioapplications, such as cell and protein chips.

• Korean journal of food and cookery science
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• v.5 no.2
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• pp.9-17
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• 1989

This study was carried out in order to study the emulsifying properties of kidney bean protein isolate. Kidney bean protein isolate was tested for the purpose of finding out the effect of pH, addition of NaCl, and heat treatment on the solbulity and emulsion capacity, emulsion stability, surface hydropobicity and emulsion viscosity. The results were summarized as follows. 1 The solubility of kidney bean protein isolate was affected by pH and showed the lowest value at pll 4.5 which is isoelectric point of kidney bean isolate. When the kidney bean protein isolate was heated, the highest value observed at pH 2 and pH 7 was 96.11%, 97.41% respectively. 2. The emulsion capacity of kidney bean protein isolate was not significantly different with each pH. With addition of NaCl, emulsion capacity decreased steadily. When heated thr highest value observed at pH 2 and pH 7 was 82.91 ml oil/100 mg protein ($60^{\circ}C$), 82.08 m1 oil/100 mg protein ($80^{\circ}C$) respectively. 3. The emulsion stability was significantly higher at pH 4.5 than that of pH 2 and pH 7 (p 0.05) When NaCl was added, emulsion stability was generally increased after 2hrs. When heated, the highest value observed at pH 2 and pH 7 was 21.25% ($80^{\circ}C$),23.7%($100^{\circ}C$) respectively after 2hrs. 4. Surface hydrophobicity increased sharply as 0.2 M NaCl was added to pH 4.5. When heated, the surface hydrophobicity increased as the temperature increased. 5. The highest value of emulsion viscosity was observed at pH 4.5 and pH 7 when 0.2 M NaCl was added. Under heat treatment, the highest value was 48,000 cps at pH 4.5 ($40^{\circ}C$). In the case of pH 7, the highest value was 105,000 cpa at $100^{\circ}C$.

• Journal of Microbiology and Biotechnology
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• v.20 no.4
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• pp.749-756
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• 2010

In many conditions, bacterial surface properties are changed as a result of variation in the growth medium and conditions. This study examined the influence of bile salt concentrations (0-0.1%) on colony morphotype, hydrophobicity, $H_2O_2$ concentration, S-layer protein production, and slpA gene expression in Lactobacillus acidophilus ATCC 4356. It was observed that two types of colonies (R and S) were in the control group and the stress condition. When the bile level increased in the medium, the amount of S type was more than the R type. A stepwise increment in the bile concentration resulted in a stepwise decline in the maximum growth rate. The results showed that hydrophobicity was increased in 0.01%-0.02% bile, but it was decreased in 0.1% bile. Treatment by bile (0.01%-0.1%) profoundly decreased $H_2O_2$ formation. S-Layer protein and slpA gene expression were also altered by the stress condition. S-Protein expression was increased in the stress condition. The slpA gene expression increased in 0.01%-0.05% bile and it decreased in 0.1% bile. However, we found that different bile salt concentrations influenced the morphology and some surface properties of L. acidophilus ATCC 4356. These changes were very different in the 0.1% bile. It appears that the bacteria respond abruptly to 0.1% bile.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.10
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• pp.1668-1675
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• 2004

The effect of pH on surface hydrophobicity, sulfhydryl group, infrared spectrum, SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) pattern and enthalpy was investigated in recovered protein from mackerel and frozen blackspotted croaker by alkaline processing. Hydrophobic residue in myofibrillar protein exposed to the surface of protein, and hydrophobic interaction were the highest around 6$0^{\circ}C$. The surface hydrophobicity was different between myofibrillar protein and myofibrillar protein including sarcoplasmic protein (recovered protein). The peak at 1636 c $m^{-l}$ was increased with pH, and the recovered protein was unfolded in alkali pH. Difference of surface and total sulfhydryl group at pH 7.0 and 10 was comparative high, and decrease of surface sulfhydryl group indicated formation of S-S bonds. Mackerel and frozen blackspotted croaker in alkaline pH showed bands of polymerized myosin heavy chain on SDS-PAGE pattern. The transition temperatures of recovered protein were 33.1, 44.3 and 65.5$^{\circ}C$. Gelation of recovered protein from alkali processing was estimated by increase of $\beta$-sheet structure by pH treatment, S-S bonds by oxidation of surface sulfhydryl group in heating, polymerization of myosin heavy chain in order.r.

• Food Science of Animal Resources
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• v.38 no.5
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• pp.1101-1108
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• 2018

The aim of this study was to investigate the effects of dry-aging (DA) and the cooking process on the myofibril protein functionalities and in vitro digestibility of proteins in beef loin. Six sirloins from beef were dry-aged for 28 d, and the control group (n=6) was analyzed 2 d postmortem for this study. Dimensional changes (reduction of thickness and surface shrinkage) after cooking were significantly greater in the control group than the DA group, whereas the shear force of the DA group was significantly lower than that of the control. Effect of cooking on aggregation, hydrophobicity, and in vitro digestibility were significantly higher in the DA group than in the control. After cooking, the protein in DA sirloins was more oxidized than in the control samples. According to the sodium dodecyl sulfate-polyacrylamide gel electrophoresis result, the low molecular weight bands (below 17 kDa) increased in the DA group, finding that the protein characteristics of dry-aged beef was affected by cooking.

• Food Science of Animal Resources
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• v.39 no.4
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• pp.576-584
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• 2019

This study was performed to evaluate the physicochemical properties of myofibrillar protein (MP) gels containing pork skin gelatin at different salt concentrations. MP gels were prepared to the different salt levels (0.15, 0.30, and 0.45 M) with or without 1.0% of pork skin gelatin. Cooking yield (CY), gel strength, shear stress were measured to determine the physical properties, and SDS-polyacrylamide gel electrophoresis, scanning electron microscopy, fourier transform infrared spectroscopy, sulfhydryl group and protein surface hydrophobicity was performed to figure out the structural changes among the proteins. The addition of gelatin into MP increased CYs and shear stress. MP at 0.45 M salt level had the highest CY and shear stress, as compared to MPs at lower salt concentrations. As the salt concentration of MP gels increased, the microstructure became the compact and wet structures, and decreased the amount of ${\alpha}-helix$/unordered structures and ${\beta}-sheet$. MP with gelatin showed a decreased amount of ${\alpha}-helix$/unordered structures and ${\beta}-sheet$ compared to MP without gelatin. The addition of gelatin to MP did not affect the sulfhydryl group, but the sulfhydryl group decreased as increased salt levels. MP mixtures containing gelatin showed a higher hydrophobicity value than those without gelatin, regardless of salt concentration. Based on these results, the addition of gelatin increased viscosity of raw meat batter and CY of MP gels for the application to low salt meat products.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.34 no.4
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• pp.320-326
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• 2001

To obtain the basic data for preparing edible or biodegradable film, fish meal protein isolates (FMPI) were prepared through alkaline extraction. And FMPI's properties and the ester compounds permeability of FMPI film were measured. FMPI were extracted under various extracting time with 0.2 N NaOH solution at $60^{\circ}C$, Recovery ratios of FMPI extracted from fish meal were increased with extracting time increasing. Surface hydrophobicity of FMPI extracted for 1 hr showed highest value. Emulsifying activity index (EAI) was increased with the increasement of extracting time but its emulsifying stability index (ESI) showed an inverse results. Viscosity of FMPI solution showed the highest value at pH 2 but showed the lowest value at pH 4, The higher concentration of sorbitol as plasticizer showed the higher ethyl acetate permeability of FMPI film, Ethyl acetate permeability of FMPI films according to kind of plasticizers showed different degree and increased in order as follow: polyethylene glycol, glycerol and sorbitol. Ester compounds having the lower molecular weight showed the higher permeability. Increment of temperature increased the ethyl acetate permeability of FMPI film. FMPI haying higher surface hydrophobicity made FMPI film be higher tensile strength. On elongation of FMPI films, kinds of plasticizer were more effective than surface hydrophobicity of FMPI.

• Bulletin of the Korean Chemical Society
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• v.25 no.7
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• pp.1031-1035
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• 2004

The adsorption kinetics of ${\beta}$-casein on a hydrophobic surface has been studied by means of the quartz crystal microbalance (QCM). The self assembled monolayer of 1-octadecanethiol on a gold coated quartz crystal was used as a hydrophobic surface for adsorption. The adsorption kinetics was monitored in different solution conditions. Formation of monolayer is observed in most cases. At high concentration of protein, micelle formation which is interrupted by high ionic strength of solution is observed. Casein binding cations such as $Ca^{2+},\;Ba^{2+}\;and\;Al^{3+}$ increase the hydrophobicity of the protein and the multiple layer adsorption occurs. The strong and weak points of the QCM method in the study of protein adsorption are discussed.

• 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.

• Preventive Nutrition and Food Science
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• v.4 no.2
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• pp.139-144
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• 1999

Lipoprotein lipase (LPL) I san enzyme that catalyzed the hydrolysis of triacylglycerols of chylomicrons and VLDL to produce 20acylglycerols and fatty acids. The enzyme, LPL, is localized on the surface of the capillary endothelium and is widely distributed in extrahepatic tissues including heart, skeletal muscle and adipose tissue. LPL has been isolated from boving milk by affinity chromatography on heparin-separose in 2 M NaCL, 5mM barbital buffer, pH 7.4. To elucidate the lipid-binding regin, LPL was digested with trypsin and then separated by gel filtration. Lipid binding region of LPL has been investigated by recombining LPL peptides with DMPC vesicles. Proteolytic LPL fragments with DMPC were reassembled and stabilized by cholate. Lipid-binding region of LPL was identified by a PTH-automated protein sequencer, as AQQHYPVSAGYTK. The analysis of the secondary structure of the lipid-binding peptides revealed a higher probability of $\alpha$-helix structure compared to the whole LPL protein. The prediction of hydrophobicity of lipid -binding region was highly hydrophobic (-1.1) compared to LPL polypetide(-0.4).