• Journal of Korean Ophthalmic Optics Society
• /
• v.15 no.3
• /
• pp.227-234
• /
• 2010

Purpose: The cleaning effect of protein deposit and the change of contact lens parameters by ultrasonic cleaner for eye glasses on the soft contact lenses were investigated. Methods: Etafilcon A contact lenses contaminated with protein, was ultrasonicated by ultrasonic cleaner for eye glasses and for the control group, spoiled contact lenses were cleaned by multi-purpose solution. The remaining protein deposits on the contact lenses were determined after extraction and the changes of overall diameter, base curve, center thickness power, and water contents on contact lenses were measured and surfaces of contact lenses were observed by scanning electron microscope. Results: The cleaning efficacies of multi-purpose solution on protein deposited etafilcon A contact lenses were 6.08%, and 23.73~33.92% in the group of ultrasonic cleaner for eye glasses with multi-purpose solution and 0~12.99% in the group of ultrasonic clear for contact lens with multipurpose solution depending on the treatment time. The changes of parameters and surface on contact lenses by ultrasonication were not observed. Conclusions: Ultrasonic cleaner for eye glasses can be used to eliminate protein deposits for the diagnostic soft contact lens in the office since it was effective to eliminate protein deposits and not caused change of parameters on soft contact lenses.

• Applied Biological Chemistry
• /
• v.30 no.3
• /
• pp.234-241
• /
• 1987

Conditions necessary for optimal plastein productivity from sardine protein hydrolysate using papain and pepsin were established. Sardine protein concentrate was hydrolyzed with pepsin yielding an approximate degree of hydrolysis of 77.2%. Enzyme induced plastein was optimized at: pH 6 for papain and pH 4 for pepsin; substrate concentrate, 50%(w/v) for papain and 40%(w/v) for pepsin; time of incubation, 24hr; enzyme/substrate ratio, 1 : 100(w/w). Plastein yields of 49.5% and 45.3% were found for papain and pepsin, respectively, when 10% trichloroacetic acid (TCA) was used as the precipitating agent. However, when plastein was precipitated by 50% ethanol, the yield was found to be 43.6% and 41.0% for papain and pepsin, respectively. Ethanol-precipitated plastein did not contain lipid and contained approximately 1.3% ash and 91.0% protein. In comparison, the TCA-precipitated plastein contained 74.2% protein, 0.5% lipid and 15.3% ash.

• Applied Biological Chemistry
• /
• v.29 no.1
• /
• pp.83-89
• /
• 1986

To investigate effectors on the colloidal stability of whey and soybean proteins, characteristics of tofu-gel formation, effects of heat treatment and salt composition on the colloidal stability, and effects of heat treatment on storage stability were analyzed. When experimental tofus were made from the mixture of whey and soybean, the calcium in the whey precipitated the soy proteins, and disrupted the gel formation, which resulted in the curd of poor texture. In the heat treatment at $60{\sim}100^{\circ}C$, whey and the whey proteins dialyzed against distilled water were readily preciptated at over $70^{\circ}C$, but the mixture of whey and soy extract as well as soy extract were stable at the range of temperature. The proteins of soy extract, whey dialyzed against sodium phosphate buffer, and the mixture were stable at the same heat treatment, and this suggested that phosphates in the soy extract stabilize specialty the whey proteins. Soy proteins were easily destabilized by adding $CaCl_2(0.05{\sim}0.07M)$ at $80{\circ}C$ and $70{\sim}85%$ of the proteins in soy extract and the mixture were preciptated, while only $30{\sim}55%$ of the proteins in whey dialyzed against distilled water were destabilized at the same conditions. Storage stability at $4^{\circ}C$ of the mixture was increased when the mixture was treated at $63^{\circ}C$ and lower temperature.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.43 no.9
• /
• pp.1462-1466
• /
• 2014

In this study, an attempt was made to produce oat protein concentrates from defatted oat groat by alkali extraction. Independent variables formulated by D-optimal design were NaOH concentration (X1, 0.005~0.06 N) for extraction and precipitation pH (X2, pH 4.0~6.0), and the dependent variable was extraction yield (Y1, %). Experimental results were analyzed by response surface methodology to determine optimized extraction conditions. Extraction yield increased both with an increase in NaOH concentration of the extraction solution and when approaching a precipitation pH of 4.9, and NaOH concentrations were a major influencing parameter. Solubility of oat protein concentrates showed a minimum value (i.e., 0.1%) at pH 5 and increased substantially at pH values in the range of ${\leq}$ pH 3 or ${\geq}$ pH 7, reaching a maximum value at pH 11 (i.e., 76%). Regression equation coincided well with the results of the experiment. Optimized extraction conditions to maximize extraction yield were 0.06 N NaOH (X1) for extraction and pH 4.7 (X2) for precipitation.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.21 no.3
• /
• pp.263-269
• /
• 1992

Radish green juice was used as a dual source for the production of plant protein precipitate and Candida utilis biomass. Precipitates ranging from 10.0 to 16.5g were obtained from a liter of radish green juice by heating at 80-10$0^{\circ}C$C for 1 to 10 min or by modification of the pH of radish green juice. Crude protein content of the precipitate was between 25 and 38%. The residue remaining after protein precipitation was used in turn for the cultivation of the yeast, C. utilis, in order to produce yeast biomass. C. utilis grew well in radish green residual juice and completed growth within 24 hr at 3$0^{\circ}C$ and 200rpm in shake flask experiments. Maximum dry cell weight obtainable from a liter of radish green residual juice was 19.5g, when the yeast was grown on the juice residue diluted 3 times or more with water to make sugar content be equal to or less than about 1.0%. Supplementation of 3-fold diluted radish green residual juice with yeast extract and (NH$_4$)SO$_4$ enhanced yeast biomass production and cell protein content significantly. Total high protein material obtainable from a liter of radish green juice was 33.0g.

• Korean Journal of Food Science and Technology
• /
• v.7 no.4
• /
• pp.250-253
• /
• 1975

The acid milk containing grape juice was prepared from natural grape juice, acid milk and sugar as raw materials, and the stability of the drink was studied. The following results were obtained. 1. The milk mixed with natural grape juice formed coagulated precipitate by coupling of the colloidal materials in the juice with the milk protein and the formation of precipitate was accelerated by pasteurization. 2. The pectin in natural grape juice was affected on the stability of the product, and the stability increased with decrease in the content of pectin. When the content of pectin in natural grape juice was lower than 2.5mg%, the precipitate was not formed in the drink containing 10 to 20% of the juice. 3. The acid milk drink containing the natural grape juice treated with pectinase, not formed precipitate by pasteurization at $85^{\circ}C$, for 20 minutes and can be preserved for long term.

• Applied Biological Chemistry
• /
• v.26 no.4
• /
• pp.199-204
• /
• 1983

As a way of utilizing cheese whey to fortify sulfur-bearing amino acids to soybean protein, whey-soybean coagulum was made from whey-soy milk mixture and optimum conditions for coprecipitation of the two proteins were determined. Mixture of whey and soymilk in 1 : 1 volume ratio was coagulated at $0.005{\sim}0.5M$ of $CaCl_2$ concentration, pH $1.5{\sim}8.0$, and at $60{\sim}100^{\circ}C$, and absorbance at 500nm of filtrate from the coagulum was measured. Optimum conditions for the coprecipitation were 0.0125M of $CaCl_2$ concentration, pH $6.5\sim7.5$, and $70{\sim}80^{\circ}C$ which resulted in the minimum absorbance and also good physical properties of the curd.

• Korean Journal of Food Science and Technology
• /
• v.10 no.2
• /
• pp.162-172
• /
• 1978

We have studied to develop a process for the preparation of protein isolates free of isothiocyanate and oxazolidine-thione when defatted meal was extrracted with a cold alkaline solution at pH11.0. The rapeseed protein isolates were separated at $0^{\circ}C$ using 1% sodium algiante of 500 cps as a precipitation aid, also. The proteins had original colors, namely, a grey curd at pH 6.7, a light cream at pH 5.6 and a yellow cream at pH 5.0, The purity and the color was improved by washing with water and freez-drying with acetone, not at room temperature. A countercurrent procedure was a prerequisite for a continuous large scale production of protein isolates.

• Korean Journal of Crystallography
• /
• v.14 no.1
• /
• pp.35-38
• /
• 2003

A simple multistep-concentration setting in capillaries was used to control the water-evaporation rate in vapor-diffusion protein crystallization. In the method used, a variety of evaporation rate curves were obtained by using the secondary precipitant solution referred to as “regulatory solution”, which is not directly exposed to the protein solution. The curves were applied to the crystallization of lysozyme as a model protein. The results clearly showed that crystal growth is dependent on the evaporation rate. Especially, the decoupling curves in which precipitant concentration in protein solutions increases to a certain point and then decreases to the equilibrium concentration gave the best crystals.

• Journal of Sericultural and Entomological Science
• /
• v.33 no.1
• /
• pp.1-5
• /
• 1991

PBS soluble- and insoluble-extracts form silkworm eggs were analysed by native-PAGE and SDS-PAGE. During the embroyonic development, soluble proteins which are mainly composed of ESP, vitellin and 30K proteins showed similar degradation pattern in both electrophoretic analyses. Several peptides which seemed to be intermediated forms of yolk proteins were detected in latter part of embryogenesis, while a protein band newly appeared in one day elapsed after acid treatment. When insoluble extracts from silkworm eggs were analysed with SDS-PAGE, several peptides were detected at the later stages of the embryonic development, and newly hatched larvae. These peptides are considered to be structure proteins for embryonic morphogenesis.