• Korean Journal of Food Science and Technology
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• v.20 no.6
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• pp.840-844
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• 1988

High-protein rice flour (HPRF) was prepared by an enzymatic process using ${\alpha}-amylase$ and g1ucoamylase without cooking Process and the feasibility of HPRF as infants foods was tested. Rice flour slurry was treated with 0.25% ${\alpha}-amylase$ and 0.5% glucoamylase at $55^{\circ}C$ for 24hrs. After saccharification, the digested rice slurry was centrifuged and the precipitated paste, was then heat-dried to obtain HPRF. The protein content of the HPRF was 20.8%. On the other hand, the supernatant of glucose enriched solution was decolourized, deionized and then isomerised to furctose at $60^{\circ}C$ for 100min by using immobilized glucose isomerase column. The high-fructose solution (HFS) contained 56% glucose, 42% fructose and 2% oligosaccharide. The nutritional quality of the HPRF was compared with milk protein and soybean protein in weight gain, feed efficiency ratio (FER), protein efficiency ratio (PER) and liver weight. HPRF was almost the same in all items with milk and soybean protein, but significantly superior to rice flour group.

• Korean Journal of Food Science and Technology
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• v.30 no.1
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• pp.22-34
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• 1998

The purpose of this study is to develop biosensor for determination of glucose, lactate, and ethanol in foods and food-stuffs simultaneously. The multiple cathode system was prepared with an oxygen electrode having one anode and hexagonal cathode. Glucose oxidase, mutarotase, lactate oxidase, alcohol oxidase and catalase were used for immobilization to determine glucose, lactate, and ethanol. These components including ethanol were simultaneously determined by the immobilized enzymes in the multiple cathode system. The determination of the components by enzyme sensor was based on the maximum slope of oxygen consumption from enzyme reaction of each sensor part. The response time for analysis was 1 min. The optimum condition for glucose, lactate and ethanol sensor was found to be 0.1 M potassium phosphate buffer, pH 7.0 at $40^{\circ}C$. Interferences of various sugars and organic acids were investigated. Less than 10% of error was found in determination of the components except organic acids. This difference was compensated by the modified equation. This system was confirmed by conventional methods. It was concluded that the multiple cathode system of this study is for an effective method to determine sugar, organic acid, ethanol simultaneously in foods.

• Journal of Life Science
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• v.25 no.3
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• pp.345-348
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• 2015

An organic solvent stable lipase from solvent-tolerant Pseudomonas sp. BCNU 171 had an optimal pH of 8 and an optimal temperature of 37℃. This crude extracellular lipase from BCNU 171 exhibited increased stability in the presence of various types of solvents at high concentrations (25%, v/v). The lipase stability was found to be highest in the presence of xylene (137%), followed by toluene (131%), octane (130%), and butanol (104%). Overall, BCNU 171 lipase tended to be more stable than immobilized commercial lipase (Novozyme435) in the presence of organic solvents. Furthermore, BCNU 171 lipase maintained about 90% of its enzyme original activity in the presence of NH₄⁺, Na⁺, Ba²⁺, Hg²⁺, Ni²⁺, Cu²⁺, and Ca²⁺ion and significantly increased its enzyme activity in the presence of various emulsifying agents. Thus, the organic solvent stable lipase from Pseudomonas sp. BCNU 171 could be usable as a potential whole cell biocatalyst and for synthetic applications of enzymes for industrial chemical processes in organic solvents without using immobilization.