• Journal of Food Hygiene and Safety
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• v.23 no.4
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• pp.338-342
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• 2008

Choline is important an organic compound for normal membrane function, acetylcholine synthesis, lipid transport, and methyl metabolism. In biological tissues and foods, there are multiple choline compounds that contribute to choline content. Many researches suggest that memory and intelligence are improved by the supplement of choline. Recently, according to the effects of choline for memory, choline has been added to milk. In this study, the content of choline was analyzed the commercial whole milks and flavored milks by enzymatic method. The standard curve was linear with 0.00316 slope and 0.994 correlation coefficient. Recoveries varied between 89.8 and 97.6%. Contents of choline in whole milks and flavored milks were 14.56-15.19 and 4.11-11.50 mg/100g, respectively. The results of this study may be usable for the establishment of choline adequate intake for Korean.

• Korean Journal of Food Science and Technology
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• v.37 no.6
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• pp.1024-1027
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• 2005

Rapid and simple method was developed for simultaneous determination of vitamins $D_3\;and\;K_1$ contents in infant formula. Contents of vitamins $D_3\;and\;K_1$, extracted by column-switching HPLC with reversed phase column using enzymatic hydrolysis and organic solvent, in CRM determined by developed method were within certified ranges of standard values.

• Food Engineering Progress
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• v.15 no.1
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• pp.41-47
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• 2011

The defatted rice bran (DRB) was enzymatically hydrolyzed using eight commercial proteases for 4hr at optimum pH and temperature. Proteolytic hydrolysates were examined in supernatant and precipitate using lowry, semimicro kjeldahl and gravimetric method using weight difference before and after enzymatic hydrolysis. In lowry and kjeldahl protein assay method, two proteases (Alcalase and Protease N) were found to be the most effective enzymes. In gravimetric method, 60.6~118.3 mg protein/g DRB was hydrolyzed after eight commercial proteases treatments. Similar to lowry and kjeldahl method, 118.3 and 107.1 mg protein/g DRB were hydrolyzed after Alcalase and Protease N treatments, respectively. When two or three effective proteases (Protamex, Alcalase and Protease N) were applied at one time to obtain synergistic effect, significant increase (P<0.05) was observed when three proteases were applied at one time (63.4 mg protein/g DRB in lowry method and 204.5 mg protein/g DRB in gravimetric method). This result suggests that Alcalase and Protease N were the most effective enzymes for proteolysis of DRB and three commercial enzymes (Protamex, Alcalase and Protease N) showed the synergistic effect on the hydrolysis of DRB.

• BMB Reports
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• v.35 no.3
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• pp.302-305
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• 2002

Kinetic and thermodynamic studies have been made on the effect of the inosine product on the activity of adenosine deaminase in a 50 mM sodium phosphate buffer, pH 7.5, at $27^{\circ}C$ using UV spectrophotometry and isothermal titration calorimetry (ITC). A competitive inhibition was observed for inosine as a product of the enzymatic reaction. A graphical-fitting method was used for determination of the binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to $140\;{\mu}M$ by the microcalorimetry method, which agrees well with the value of $143\;{\mu}M$ for the inhibition constant that was obtained from the spectroscopy method.

• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.5
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• pp.794-799
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• 1997

The effective fermentation methods of Kimchi juice for utilization of outer layer of Chinese cabbage, an waste of Kimchi industry were studied. The Kimchi juice prepared with brining and grinding the waste of Chinese cabbage and addition of spices was fermented at $25^{\circ}C$. Addition of 5$^{\circ}C$15% fermented Kimchi juice of pH 5.4 at initial stage and pH 4.4 at middle state resulted in a significant increase in fermentation rate and solid content after 12 hours of fermentation. The combined method of enzymatic hydrolysis(0.1% viscozyme) of the brined and ground cabbage and addition of 2.0% NaCl, 1.0% sucrose and 10% fermented juice of pH 5.4 first and 4.4 during fermentation, respectively resulted in more rapid fermentation. The solid concentration was 5 times higher than control at maximum point and acidic and total flavor intensity were also significantly high.

• YAKHAK HOEJI
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• v.45 no.3
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• pp.245-250
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• 2001

Aminoacyl tRNA synthetases of bacteria are known as potential targets for new anti-microbial agents. To isolate new inhibitors of bacterial methionyl-tRNA synthetases from natural sources, a new target-oriented screening system using whole cells which are over-expressing a target enzyme was developed. Approximately 8,000 culture broths of microorganisms from soils were tested by this screening system. Among them, ten culture broths was found to contain inhibitory activity against methionyl -tRNA synthetases of Escherichia coli. For the validation of the screening system, this new method was compared with in vitro enzymatic method. Seven out of 10 culture broths showed inhibitory activity against methionyl-tRNA synthetases of E. coli. This result showed that the new screening system was comparable to the enzyme assay. Thus we believe that our screening system as a new method can be applied for the screening of new antibiotics inhibiting bacterial methionyl-tRNA synthetases from natural products.

• KSBB Journal
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• v.5 no.2
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• pp.191-194
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• 1990

Tyrosine is a monohydrolic aromatic amino acid and DOPA is a tyrosine derivative containing dihydroxy group. DOPA can be synthesized from tyrosine by enzymatic reaction. The separation and quantitative determination of each component are very difficult in the reaction mixture. In the present study, two wavelengths giving maximum absorbance difference of each amino acid were determined using UV/VIS spectrophotometer by wavelength scanning and simple assay method was developed for the analysis of the reaction mixture of tyrosine and DOPA by measuring absorbances of reaction mixture. This method can be simply used for the analysis of the tyrosine and DOPA mixture because it does not require and procedure for the pretreatment of the reaction mixture.

• Journal of Microbiology and Biotechnology
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• v.28 no.7
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• pp.1141-1146
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• 2018

2'-Fucosyllactose (2'-FL) is one of the most important human milk oligosaccharides and has several health benefits for infants. The levels of 2'-FL in breast milk or samples from other sources can be quantified by high-performance liquid chromatography. However, this method cannot be used for simultaneous detection of the target compound in numerous samples. Here, we developed a simple method for quantifying 2'-FL in a microplate format. The method involves two steps: (i) release of $\text\tiny{L}$-fucose from 2'-FL by ${\alpha}$-(1-2,3,4,6)-$\text\tiny{L}$-fucosidase and (ii) measurement of NADPH formed during the oxidation of $\text\tiny{L}$-fucose by $\text\tiny{L}$-fucose dehydrogenase. This method enables measurement of up to 5 g/l 2'-FL in 50 min using a 96-well microplate. The efficiency and simplicity of the proposed method make it suitable for the analyses of a large number of samples simultaneously.

• Journal of Ginseng Research
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• v.9 no.2
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• pp.154-162
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• 1985

We report a newassay method on the measurement of the catalase activity, whose utilzation value is considered to be remarkable in the field of plant biochemistry. We named this method as a De-Coupling method. The essence of de-coupling method is the separation between the enzyme reaction and the indicator reaction. The optimum condition of the enzyme reaction was found to be following: on addition of 1 ml of substrate (H2O2: 20mM) to the fixture of the crude extract of enzyme (volume: 0.2 ml) and the ammonium phosphate buffer (volume: 1.8 ml; 0.93 M phosphate, 1.6M NHB, 2.5 M methanol, pH 7.0). After 30, 60 and 90 seconds of the enzyme reactions are proceeded, the reactions are terminated by 25% of tai-chloro-acetate (final concentration of 5%), respectively. The precipitated materials by tai-chloro-acetate was removed by the centrifugation (2000g, 10minutes). Formaldehyde produced in the enzymatic reaction was reacted with 2ml of acetylacetone (60mM). The indicator reaction -(HANTSCH REAKT10N)- in which lutidine is formed, was proceeded for 60 minutes at $25^{\circ}C$.

• Microbiology and Biotechnology Letters
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• v.2 no.2
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• pp.63-77
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• 1974

The optimal operation problem of enzyme reactor of double inhibitions are dealt with Maximum Principle and Steepest Ascent Method. The operation policy of the intial concentration and amount of substrate, reaction time and the method of cross feed of substrate are determined in a system of reactor of constant volume add with cross feed of substrate. The policy for the soluble enzyme and the immobilized enzyme are greatly different from each other, and the performance index, the profit per unit time, of the latter are nearly twice greater than that of the former.