• Biotechnology and Bioprocess Engineering:BBE
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• v.9 no.4
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• pp.241-244
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• 2004

Protein A molecular thin film was fabricated as a platform of antibody-based biosensor. For the immobilization of the protein A thin film, a viologen multilayer was built up using the Langmuir-Blodgett (LB) technique, and then, protein A was adsorbed on the viologen LB film by an electrostatic interaction force, which was formed as a hetero-film structure. For the deposition of viologen, surface pressure area ($\pi$-A) isotherm was investigated. The fabricated protein A-viologen hetero LB film was investigated using atomic force microscopy (AFM). Using the developed molecular film, antibody immobilization and fluorescence measurement was carried out.

• KOREAN JOURNAL OF PACKAGING SCIENCE & TECHNOLOGY
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• v.25 no.1
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• pp.1-10
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• 2019

Environmental evaluation of two different oxygen high barrier films were performed using life cycle assessment. One of the films (traditional film) was composed of aluminum oxide coated PET film, ink, LDPE and LLDPE. Another film (new film) was consists of PET, ink, protein based coating material, LDPE, LLDPE. Main layer to achieve the high oxygen barrier for traditional film was aluminum oxide coated PET film, whereas the protein based coating material act as oxygen barrier layer for new film. Functional unit of this study was 1000 pouches made of traditional and new film. System boundary was factory to gate. The results of this study revealed that the new film shows better environmental performance for most of impact indicator than traditional film, except marine eutrophication and fine particulate matter formation due to extra coating process in new film system.

• Food Science and Preservation
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• v.10 no.3
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• pp.411-416
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• 2003

An effort was attempted to utilize an under-utilized protein source, rice bran protein, in coating or wrapping food material for the purpose of protection them from oxidation and bacterial infection. However, the utilization of rice bran protein as a food coating material is limited because the rice bran protein coating material itself can be spoiled by a bacterial infection. Therefore, this study was conducted to produce the economical and antibacterial rice bran protein film by utilizing rice bran and bacteriocin-producing microorganism. Bacteriocin produced by Pseudomonas putida 21025 was partially purified after 33h of shaking incubation at 30$^{\circ}C$. The amount of amino-type nitrogen did not increase in the rice bran protein film containing the bacteriocin any more after gradual increase upto the content of 0.22％ for 8 days, while that without the bacteriocin increased continuously, implying that application of the bacteriocin to the rice bran had positive effects on prolonging the shelf-life of not only film itself but also the foods wrapped by this film.

• Journal of Microbiology and Biotechnology
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• v.16 no.4
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• pp.597-604
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• 2006

In order to extend the shelf-life of packaged or coated foods, an antibacterial edible film containing 1.8% of BLS was developed from the defatted corn germ meal, which had been fermented with Bacillus subtilis under the optimum condition of pH 7.0-7.5 and $33^{\circ}C$ for 33 h. Water vapor permeability of the fermented film $(88.3mg/cm^2\;h)$ was higher than those of the normal corn germ films $(75.8mg/cm^2\;h)$. Protein solubility of the fermented film was also higher than ordinary corn germ film at the pH range of 3-10. The fermented corn germ film had higher tensile strength and lower % elongation (elongation rate) than the ordinary corn germ film. The antimicrobial activity of the film was more than 50% of the maximum activity after film production with heat treatment at $90^{\circ}C$ and pH adjustment to 9. When the corn germ protein film with bacteriocin-like substance was applied on the mashed sausage media containing E. coli, the bacterial growth inhibition was higher than the ordinary corn protein film.

• Food Science of Animal Resources
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• v.35 no.5
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• pp.611-614
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• 2015

This study was performed to apply a protein film containing a natural antimicrobial compound to meat packaging and determine quality change of meat during storage. Proteins obtained from the by-products of food processing have been utilized as biodegradable film sources. Porcine meat and bone meal (MBM) is obtained during meat processing, and proteins from the MBM can be extracted and used as a film base material. Previously, an antimicrobial MBM film containing coriander oil (CO) was prepared and its physical properties and antimicrobial activity were characterized. In this study, the antimicrobial MBM-CO film was applied to beef patties packaging, and the microbial population and the degree of lipid oxidation were determined during storage at 4℃ for 15 d. The population of inoculated E. coli O157:H7 in the samples wrapped with the MBM-CO film was 6.78 log colony forming unit (CFU)/g after 15 d of storage, whereas the control had 8.05 Log CFU/g, thus reducing the microbial population by 1.29 Log CFU/g. In addition, retardation of lipid oxidation in the patties was observed during storage for the samples packaged by the MBM-CO film, compared with the control samples. These results suggest that the MBM-CO film can be useful for enhancing the quality of beef patties during storage.

• Preventive Nutrition and Food Science
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• v.13 no.4
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• pp.370-374
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• 2008

The Gelidium corneum (GC)-whey protein isolate (WPI) blend film containing grapefruit seed extract (GSE) was prepared by incorporating different amounts (0, 0.02, 0.04, 0.08, 0.1%) of GSE into the film. The film's tensile strength (TS) and water vapor permeability (WVP) were improved by the addition of GSE. The film containing 0.1% GSE had a TS of 3.27 MPa, whereas the control had 2.64 MPa. WVP of the film was also significantly decreased by the addition of GSE. Addition of 0.1% GSE decreased the populations of Escherichia coli O157:H7, Listeria monocytogenes, and Salmonella Typhimurium by 1.0, 1.6, and 0.6 log CFU/g, respectively, compared to the control. Fish paste was packed with the GC-WPI blend film containing GSE, and microbial change in the fish paste inoculated with E. coli O157:H7, L. monocytogenes, and S. Typhimurium during storage was examined. Populations of E. coli O157:H7, L. monocytogenes, and S. Typhimurium were decreased by 0.60, 0.48, and 0.85 log CFU/g, after 7 day of storage, respectively. These results suggest packaging fish paste in the GC-WPI blend film containing GSE can extend the shelf life.

• Food Science and Biotechnology
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• v.18 no.4
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• pp.889-894
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• 2009

Barley proteins are expected to have unique functional properties due to their high content of alcohol soluble protein, hordein. Since the barley proteins obtained by conventional isoelectric precipitation method cannot represent hordein fraction, barley proteins were fractionated to albumin, globulin, glutelin, and hordein with respect to extraction solvents. Functional properties and film-forming properties of solubility-fractionated barley proteins were investigated to explore their potential for human food ingredient and industrial usage. The 100 g of total barley protein comprised 5 g albumin, 23 g globulin, 45 g glutelin, and 27 g hordein. Water-binding capacities of barley protein isolates ranged from 140-183 mL water/100 g solid. Hordein showed the highest oil absorption capacity (136 mL oil/100 g), and glutelin showed the highest gelation property among the fractionated proteins. In general, the barley protein fractions formed brittle and weak films as indicated by low tensile strength (TS) and percent elongation at break (E) values. The salt-soluble globulin fraction produced film with the lowest TS value. Although films made from glutelin and hordein were dark-colored and had lower E values, they could be used as excellent barriers against water transmission.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.33 no.5
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• pp.413-417
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• 2000

The effects of film processing conditions on the water vapor permeability (WVP), the solubility of film's protein (SFP) and the soluble film's meterials amount (SFMA) were investigated to establish the conditions for preparing biodegradable and edible Alaska Pollack meal protein isolate (APMPI) film. ms of film were decreased with increasing plasticizer concentration but those were decreased with decrement of APMPI's pH values. SEPs were decreased with increasing APMPI's pH and plasticizer concentration. SFMAS were also strongly affected by plasticizer concentration and APMPI's pH. In the case of adding different plasticizers, WVP was increased in order as follows: glycerol, polyethylene glycol and sorbitol but SFMA showed inverse order.

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.859-862
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• 2001

For the development of preferable immunosensor and protein chip, the viologen Langmuir-Blodgett (LB) multilayer was fabricated on the surface, and then protein A was adsorbed on the proposed viologen LB film by electrostatic attractive force. The Immunoglobulin G (IgG) labeled with fluorescence marker was self-assembled on the fabricated protein A film. The topographies of the deposited films were investigated by using atomic force microscope (AFM). The immobilization of IgG was verified by fluorescence spectrum. Such structures can be used as sublayers for various kinds of IgG immobilization toward immunosensors and protein chip.

• Korean Journal of Food Science and Technology
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• v.30 no.2
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• pp.372-378
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• 1998

Two types of formaldehyde-treated soy protein isolate (SPI) films, formaldehyde-incorporated and formaldehyde-adsorbed films, and control SPI films were prepared. Cross-linking effect of formaldehyde on selected film properties such as color, tensile strength (TS), elongation at break (E), water vapor permeability (WVP), and water solubility (WS) were determined. Physical properties of formaldehyde-incorporated films were not geneally different from those of control films, while almost all of those among formaldehyde-adsorbed films were significantly different. Through cross-linking development within formaldehyde-adsorbed films, WS decreased significantly (P<0.05) from 26.1% to 16.6%, and TS increased two times while E decreased two times compared with control films. This was caused by insolubilization and hardening of protein by cross-linking most likely attributed to the significant changes in properties of protein films reacted with formaldehyde.