• Journal of the Korean Chemical Society
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• v.37 no.2
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• pp.213-219
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• 1993

The electrochemical spectral sensitization of $SnO_2$ electrodes with rhodamine B was studied. Photocurrent was measured in the presence of a variety of supersensitizers including ascorbic acid and KI. In the presence of ascorbic acid, the increase in the concentration of ascorbic acid, pH of the solution, or the potential applied to $SnO_2$ up to 0.6 V vs. SCE enhanced the photocurrent. However, ascorbic acid produced considerably high dark current due to its low reduction potential. On the other hand, KI produced low but stable photocurrent. The results, together with the solvent effect on the photocurrent, were taken into account to elucidate the mechanism of photosensitization in the presence of ascorbic acid or KI.

• Journal of Microbiology and Biotechnology
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• v.16 no.1
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• pp.64-67
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• 2006

To enhance the stability of ascorbic acid, the glycosylation of ascorbic acid was studied using the transfructosylation activity of levan fructotransferase. When levan was used as glycosyl donor, a novel fructoside (ascorbic acid 2-ffuctoside) was formed by the transfructosylation activity of the levan fructotransferase. The production of ascorbic acid 2-fructoside was highly affected by the concentration of the fructosyl acceptor (ascorbic acid). When $35\%$ of ascorbic acid and $2\%$ of levan were incubated with LFTase of 0.5 unit/glevan at $37^{\circ}C$ for 85 h, a maximum 52 g/l of AA-2F was produced.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.50 no.6
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• pp.457-461
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• 2005

During the last few years, considerable progresses have been made in understanding of roles and biosynthesis of ascorbic acid (AsA) in plants. The concentrations of ascorbic acid is 2-4 mM in leaf cells, but much higher at the chloroplast. There are three forms of ascorbic acid in the plant mainly ascorbic acid (AsA), monode­hydroascorbic acid (MDHA) and dehydroascorbic acid (DHA). AsA in plant cell performs antioxidants by changing those three forms. And AsA promotes cell division and elongation There was new pathway of ascorbic acid metabolism. It is called pathway of Smirnoff-Wheeler. This report will provide understanding of AsA in plants, and also provide

• Journal of the Korean Chemical Society
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• v.39 no.1
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• pp.29-34
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• 1995

The rates for the oxidation reaction of l-ascorbic acid by Cu(Ⅱ)-polyamine complexes were measured by Onish's method at the pH 4.6. The oxidation process of l-ascorbic acid is proposed to occur by the inner-sphere mechanism that involves the formation of a Cu(Ⅱ)-ascorbic acid complex and electron transfer at the rate-determining step.

• Archives of Pharmacal Research
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• v.11 no.2
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• pp.114-121
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• 1988

To gain insight into possible cellular protective mechanisms against the insult of formaldehyde, we have investigated this molecule's reactivity with both naturally occurring thiol compounds including glutathione and L-ascorbic acid. By UV measurements, for maldehyde was found to rapidly react with glutathione forming an S-hydroxymethyl covalent adduct. The adduct which was confirmed by NMR is transiently stable. Formaldehydissimilar to its reaction with dimedone. The reaction of formaldehyde with glutathione was reduced by 40% in the presence of an excess amount of L-ascorbic acid, due to the trapping of formaldehyde by L-ascorbic acid. The data suggest that L-ascorbic acid may have a possible in vivo role in the metabolism of formaldehyde, thereby protecting cellular glutathione from possible depletion.

• Journal of Microbiology and Biotechnology
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• v.8 no.6
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• pp.710-713
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• 1998

A material with the same high performance liquid chromatography (HPLC) retention profile as authentic ascorbic acid 2-Ο-$\alpha$-glucoside (AA-2G) was detected in kimchi. This material was identified as AA-2G by testing its susceptibility to $\alpha$-glucosidase hydrolysis, the HPLC profile, and through the elementary analysis. Among several strains of bacteria isolated from fermented kimchi, four strains could produce cydodextrin glucanotransferase (CGTase) which catalyzes the transglucosylation reaction of ascorbic acid. By using starch as the glycosyl donor, AA-2G was produced as the major product through this reaction.

• Food Science of Animal Resources
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• v.37 no.2
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• pp.288-296
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• 2017

We investigated the effects of fermented red beet extract and ascorbic acid on color development in meat emulsions. The pH of meat emulsions containing red beet extract decreased with an increase in the amount of extract added. The redness of the treated meat emulsions was higher than that of the control with no added nitrite or fermented red beet extract (p< 0.05), though the redness of the meat emulsions treated with fermented red beet extract only was lower than in that treated with both fermented red beet extract and ascorbic acid (p<0.05). The highest VBN, TBARS, and total viable count values were observed in the control, and these values in the meat emulsions treated with fermented red beet extract were higher than in that treated with both fermented red beet extract and ascorbic acid (p<0.05). E. coli and coliform bacteria were not found in any of the meat emulsions tested. Treatment T2, containing nitrite and ascorbic acid, had the highest overall acceptability score (p<0.05); however, there was no significant difference between the T2 treatment and the T6 treatment, which contained 10% pre-converted nitrite from red beet extract and 0.05% ascorbic acid (p>0.05). The residual nitrite content of the meat emulsions treated with ascorbic acid was lower than in those treated without ascorbic acid (p<0.05). Thus, the combination of fermented red beet extract and ascorbic acid could be a viable alternative to synthetic nitrite for the stability of color development in meat emulsions.

• Applied Biological Chemistry
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• v.36 no.2
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• pp.86-92
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• 1993

Myrosinase from radish was purified by DEAE Bio-Gel, Con-A, and Superose-6 column. The purified myrosinase(II) possessed 2 subunits, and their molecular as determined by SDS-polyacrylamide gel electrophoresis were 53 and 39 KD, respectively. The specific activity of purified enzyme was 37,500 units/mg. The enzyme was purified approximately 44-fold compared to the crude enzyme. Optimum pH of the myrosinase was $6.5{\sim}7.0$ in phosphate and Tris-HCl buffer solutions. Optimum temperature of the enzyme was $37{\sim}38^{\circ}C$. The enzyme was stable at pH 7.0, and less than $30^{\circ}C$. Cu or Hg ion significantly inhibited the enzyme activity, but ascorbic acid enhanced, resulting in a maximum activity by 1 mM ascorbic acid. Among the ascorbic acid analogues, dehydroascorbic acid did not affect, whereas others showed a little effect, but less than ascorbic acid itself. Individual 2-mercaptoethanol and dithiothreitol (reducing agents) did not enhance the enzyme activity. but 2-mercaptoethanol effect was enhanced when mixed with ascorbic acid.

• Proceedings of the PSK Conference
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• 2002.10a
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• pp.279.2-280
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• 2002

Ascorbic acid is very well known as one of various ntioxidants and is used very popular in man. Melatonin. an endogenous compound secreted by the pineal gland in human brain has been reported to act as an antioxidant nowadays. The present study was performed to obtain the differences of the radioprotective function of ascorbic acid and combination with melatonin according to the administration dose a day on radiation induced DNA damage in mouse spleen and blood. (omitted)

• Applied Biological Chemistry
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• v.43 no.1
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• pp.12-17
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• 2000

For the enzymatic production of $2-O-{\alpha}-D-glucopyranosyl-L-ascorbic$ acid (AA-2G) from ascorbic acid, rice seed was used as the source of ${\alpha}-glucosidase$ having transglucosylation activity. Among six rice varieties, cultivated in Korea, ${\alpha}-glucosidase$ activity of Oryza savita L. cv. Ilpumbyeo was the highest with 125.03 unit/ml and it had maximum specific activity with 8.52 unit/mg protein when rice seeds were grown for 3 days after germination. For the production of AA-2G using crude extract of O. savita L. cv. Ilpumbyeo, maltose was most effective glucose donor. The optimum concentration of maltose and ascorbic acid were 125 mM and 175 mM, respectively. The optimum concentration of ${\alpha}-glucosidase$ was 100 unit. The most effective buffer was 100 mM sodium citrate. The optimum pH and temperature were 5.0 and $60^{\circ}C$, respectively. Under the optimum condition, $108.43\;{\mu}M/unit$ of AA-2G was produced from ascorbic acid after 35 minutes of reaction, which corresponds to 6.2% of conversion ratio based on the amount of ascorbic acid used.