• Applied Biological Chemistry
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• v.48 no.3
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• pp.228-232
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• 2005

A yeast strain producing phytase, isolated from a mash of Korean traditional Yakju, was identified as a strain of Saccharomyces cerevisiae and designated as Saccharomyces cerevisiae CY strain. Phytase was produced by CY strain both intracellularly and extracellularly. Total phytase activity by the shaking culture was about two times higher than that of the static culture. The portion of extracellular phytase to total phytase activity ranged between 23 and 49 percent, depending on the glucose concentration in the culture medium. Phytase production was reached at approximately 1 U/ml as total phytase activity and the maximum intracellular phytase activity was 0.17-0.19 U/mg-DCW at late logarithmic growth phase. The optimum reaction pH and temperature of intracellular phytase were 3.5 and $40^{\circ}C$, respectively. Over 95% of the phytate was degraded by growing cells after 36 hours yeast cell culture and about 90% of total phytate was effectively degraded by suspending the whole cell with the biomass of 0.4 mg-DCW/ml-reaction solution after 12 hours degradation reaction.

• Microbiology and Biotechnology Letters
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• v.34 no.2
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• pp.121-128
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• 2006

The purified xylanase from Bacillus alcalophilus AX2000 was modified with various chemical modifiers to determine amino acid residues in the active site of the enzyme. Treatment of the enzyme with group-specific reagents such as carbodiimide or N-bromosuccinimide resulted in complete loss of enzyme activity. These results suggested that these reagents reacted with glutamic acid or aspartic acid and tryptophan residues located at or near the active site. In each case, inactivation was performed by pseudo first-order kinetics. Inhibition of enzyme activity by carbodiimide and N-bromosuccinimide showed non-competitive and competitive inhibition type, respectively. Addition of xylan to the enzyme solution containing N-bromosuccinimide prevented the inactivation, indicating the presence of tryptophan at the substrate binding site. Analysis of kinetics for inactivation showed that the loss of enzyme activity was due to modification of two glutamic acid or aspartic acid residues and single tryptophan residue.

• The Korean Journal of Mycology
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• v.38 no.2
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• pp.202-204
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• 2010

Inhibitory effect on tyrosinase activity and melanogenesis of the mycelia and mycelial culture broth of Macrolepiota procera were investigated. The methanol fraction of culture broth showed 56.6% of tyrosinase inhibitory activity and its IC50 was 8.78 mg/ml. Using Streptococcus bikiniensis for melanogenesis in vitro, the methanol extract of mycelia showed 94.0% inhibition of melanogenesis.

• Journal of Aquaculture
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• v.21 no.3
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• pp.184-189
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• 2008

Tryptic enzyme activities in the digestive glands (hepatopancreas) and digestive tracts of Pacific white shrimps Litopenaeus vannamei were assayed at three water temperature regimes. At $26^{\circ}C$, trypsin activity in the hepatopancreas was 200% higher than at $23^{\circ}C$ and 300% higher than at $20^{\circ}C$. The highest foregut trypsin activity levels showed no significant difference in the temperature regimes, but the time between peaks in foreguts and midguts shortened at higher temperature. In the midgut, the level of enzyme activity was highest at $26^{\circ}C$ regardless of the amount of ingested feed. The ratio of foregut and/or midgut dry weight to the body wet weight indicated feed movement through the digestive track directly and gave accurate account about the feeding mechanism. Maximum feed ingestion in the foregut was equivalent to 0.6% of the body weight (wet weight) at $23^{\circ}C$, 0.4% of the body weight at $20^{\circ}C$, and 0.5% of the body weight at $26^{\circ}C$. In view of the temperatures chosen for this study, although maximum ingestion was observed at $23^{\circ}C$, the shrimps showed highest enzyme activity, but lowest feed retention time at $26^{\circ}C$ and lowest enzyme activity, but highest retention time at $20^{\circ}C$.

• Journal of the Korean Chemical Society
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• v.43 no.3
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• pp.307-314
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• 1999

Ml RNA, the RNA component of RNase P from Escherichia coli, is produced by 3' processing of pre-Ml RNA, a major primary transcript of the rnpB gene. The enzyme fraction containing the processing activity was partially purified and characterized. Since exposure of the active fraction to the high salt condition results in the inactivation of the processing activity, the processing enzyme seems to be an enzyme complex composed of multiple enzymes. The enzyme fraction loses the processing activity when treated with the chemical nuclease lead(II) ion, but regains its activity by the addition of RNA isolated from the enzyme fraction itself, suggesting that an RNA molecule(s) may be essential for the processing activity. Analysis of cleavage sites produced by the partially purified enzyme fraction also implies that the 3' processing occurs by multiple enzymes and at least in two distinct pathways.

• Journal of Korean Ophthalmic Optics Society
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• v.20 no.1
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• pp.75-81
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• 2015

Purpose: The present study was conducted to investigate whether the changes in structure and activity of antioxidative enzymes, superoxide dismutase(SOD) and catalase(CAT) present in the eyes appeared when they were repeatedly exposed to UV-A, and reveal the correlation of these changes. Methods: Each enzyme solution was prepared from the standardized SOD and CAT, and repeatedly exposed to UV-A of 365 min under the condition of 30 minutes, 1 hour and 2 hours a day over 1, 2, 3, 4 and 5 days. Structural denaturation of SOD and CAT induced by repeat UV-A irradiation was confirmed by the electrophoretic analysis, and their enzyme activity was determined by the colorimetric assay using the proper assay kit. Results: SOD exposed repeatedly to UV-A showed the polymerization pattern through the electrophoretic analysis when it was repeatedly exposed under the condition of at least 1 hour a day however, the change of its activity was found to be less than 12%. On the other hand, CAT repeatedly exposed to UV-A showed reduced size of the electrophoretic band which indicated a structure denaturation and its activity was significantly decreased. In the case of that the repeat exposure time was longer, CAT activity was completely lost even though some enzyme band was shown in the electrphoretic analysis. Conclusions: From these results, it was revealed that the degree and pattern in structural denaturation of antioxidative enzymes differently appeared according to the type of enzyme, and the degree of structural denaturation was not always consistent with the reduction in enzyme activity.

• Korean Journal of Food Science and Technology
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• v.37 no.1
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• pp.95-102
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• 2005

Effects of Morus alba fruit extracts on monoamine oxidase (MAO) activity were examined in rats during and after physical exercise. Oral administration of M. alba extract (0.3 g/kg body weight) significantly increased brain MAO-A activity but decreased liver MAO-B activity when they were measured using serotonin and benzylamine as substrates. Type of physical exercises had significant effect on MAO activity. Brain MAO-A activity markedly decreased with physical activity-related stress compared to normal group, whereas Liver MAO-B activity increased up to 60 min after exercise. Lactate dehydrogenase (LDH) activity and lactate concentration in blood, clinical indices of physical exercise activities, were also determined for correlation to MAO activities. MAO-A activity of rats subjected to oral administration of M. alba extract and physical exercise increased whereas MAO-B and LDH activities, and lactate level decreased, All indices eventually recovered normal levels, These results suggest M. alba may increase capability of physical activities by modulating MAO activities during exercise.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1978.04a
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• pp.98.5-99
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• 1978

항생물질과 RNA 분해효소를 동시에 생산하는 방선균의 한 균주를 토양으로부터 분리하여 이 균주가 생산하는 RNA 분해효소의 물리화학적 성질 및 분해산물에 대해 검토하였다. 효소반응의 최적 pH 및 온도는 명명 pH 5.6과 $50^{\circ}C이었다.$ $37^{\circ}C$ 에서 90분간 열처리 시켰을 때, 이 효소의 활성은 비교적 안정하였지마는 $50^{\circ}C$ 에서 90분간 열처리 시켰을 때는 효소활성이 심하게 저하되었다. 이 효소의 활성은 $Ba^{2+}$ 에 의하여 50% 정도의 저해 작용을 나타내었지만 EDTA에 의해서는 저해되지 않았다. 이 효소에 의한 RNA분해로 이 효소가 대사산물로서 guanosine, adenosine과 밝혀지지 않은 두 가지의 핵산관연물질을 생산함을 알 수 있었다. 제2보에서는 ENase의 효소학적 성질을 검토하였으며 이후 항생물질 측면에서 검토할 예정이다.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1979.10a
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• pp.244.2-244
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• 1979

고분자 기질을 분해하는 효소의 고정화 후의 활성 yield을 높히고자 Polysaccharide의 표면에 acrylamide 및 N-hydroxysuccinimidyl acrylate을 graft 공중합 시킴으로써 긴 측쇄에 활성 ester을 가지는 새로운 carrier에 phosphiesterase을 고정화 시켰으며 이 고정화된 phosphodiesterase의 몇가지 성질을 조사하여 본래의 phosphiesterase의 성질과 비교하였다. 1) 이 Carrier에 phosphodiesterase을 직접 고정화시킨 결과 52%가 고정화되었으며 고정화된 효소는 38%의 비활성을 나타내 주었다. 2) phosphodiesterase는 이상과 같이 고정화됨으로써 최적작용 pH는 8.0부근에서 9.0부근으로 최적작용온도는 $50^{\circ}C부근에서$ $60^{\circ}C부근으로$ KM치는 1.11mg에서 2.1mg/ml로 변하였으며 열안정성은 훨씬 증가하여 본래의 phosphodiesterase의 열불활성속도상수가 0.4인데 고정화된 효소는 0.03 이었다. 또 $5^{\circ}C에서$ 수용액상태(pH 8.0 Tris buffer)로 6개월 보관후의 관존 활성은 본래의 효소가 0.2%인데 고정화된 효소는 42%로 높은 치를 나타내주었다.

• Journal of the Korean Society of Food Science and Nutrition
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• v.12 no.2
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• pp.57-61
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• 1983

The present study was undertaken to elucidate the effect of Serotonin and Norepinephrine on Aldehyde Oxidase activity in rabbit liver, in vitro. The results were as follows; 1. Aldehyde Oxidase was measured optimum substrate concentration at $5{\times}10^{-4}M$ and incubation time for 10 minutes. 2. Aldehyde Oxidase were inhibited by Serotonin and Norepinephrine. 3. It was observed that relationship between biogenic amines and substrate were competitive inhibition on Aldehyde Oxidase.