• Korean Journal of Microbiology
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• v.18 no.1
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• pp.15-19
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• 1980

In order to study on the pigment and protease of Serratia marcescens, the correlation between protease activity and pigment formation was investigated. The results are as follows ; (1) The protease activity exhibitied two pH optima 6.0 and 7.5, respectively. (2) The optimal temeprature of proteolytic activity was $45^{\circ}C$. With these-results, it is suggested that the proteolytic enzymes of Serratia masrecescens is stable at neutral pH range and more active at the high temeprature than lthat of otehr proteolytic enzymes.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.16 no.2
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• pp.147-153
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• 1983

To check the differences of the digestive enzymes by the bait habits and the proteolytic activities of the fissile extracts from the fish, omnivorous filefish (Navodon modestus), carnivorous cat shark (Scilliorhinus tarazame) and bloodsucking hag fish (Eptatretus burgeri) were sampled for this experiment. The activity of crude alkaline protease extracted from the muscle and the internal organs of the samples was determined with casein as substrate. The activity of the proteolytic enzymes showed remarkable differences by the organs of the fish. The optimum condition of the pretenses from the muscle revealed in range of pH 7.8-8.3, at $60-65^{\circ}C$, while those of the enzymes from the internal organs were at about pH 8.2, $45-55^{\circ}C$, but those of hag fish were at about pH 6.7, $45-55^{\circ}C$. The proteolytic activity of the enzyme of alimentary canal in filefish and in hag fish was 57 and 11 times stronger than that of muscle, respectively. The crude enzyme from the alimentary canal of file fish showed the strongest proteolytic activity in samples submitted and that of cat shark was the lowest. The activity of pancreatic alkaline protease in cat shark was 50 fold higher than that of muscle alkaline protease in the fish.

• Proceedings of the Korean Society of Crop Science Conference
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• 2017.06a
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• pp.270-270
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• 2017

Brown rice flour (BRF) was treated with different carbohydrases (Viscozyme, Termamyl, Celluclast, AMG, Ultraflo, and Pentopan), and then aqueous alcoholic extracts (70% ethanol) from the treated RBF were examined for their phenolic compositions and antioxidant activities (ABTS and DPPH radical scavenging activity). All the carbohydrases tested induced significant increases in ABTS radical scavenging activity (2.1-3.0 times). Moreover, These enzymes increased the amount of extractable free phenolic acids by 10-15 times, especially for ferulic and p-coumaric acid. Among the enzymes tested, Pentopan which was active in arabinoxylan hydrolysis appeared to be most effective in increasing the free phenolic acid content and ABTS radical scavenging activity than other enzymes. Enzymatic hydrolysis of cell wall polysaccharides in BRF could be used as an effective procedure for raising the amount of extractable phenolic acids and thus increasing the antioxidant activity of BRF extract.

• Journal of Microbiology and Biotechnology
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• v.20 no.2
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• pp.383-390
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• 2010

A newly isolated active producer of raw-starch-digesting amyloytic enzymes, Rhizopus microsporus var. chinensis CICIM-CU F0088, was screened and identified by morphological characteristics and molecular phylogenetic analyses. This fungus was isolated from the soil of Chinese glue pudding mill, and produced high levels of amylolytic activity under solid-state fermentation with supplementation of starch and wheat bran. Results of thin-layer chromatography showed there are two kinds of amyloytic enzymes formed by this strain, including one $\alpha$-amylase and two glucoamylases. It was found in the electron microscope experiments that the two glucoamylases can digest raw corn starch and have an optimal temperature of $70^{\circ}C$. These results signified that amyloytic enzymes secreted by strain Rhizopus microsporus var. chinensis CICIM-CU F0088 were types of thermostable amyloytic enzymes and able to digest raw corn starch.

• Molecules and Cells
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• v.43 no.2
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• pp.160-167
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• 2020

Runt-related transcription factor 2 (RUNX2) is a key transcription factor for bone formation and osteoblast differentiation. Various signaling pathways and mechanisms that regulate the expression and transcriptional activity of RUNX2 have been thoroughly investigated since the involvement of RUNX2 was first reported in bone formation. As the regulation of Runx2 expression by extracellular signals has recently been reviewed, this review focuses on the regulation of post-translational RUNX2 activity. Transcriptional activity of RUNX2 is regulated at the post-translational level by various enzymes including kinases, acetyl transferases, deacetylases, ubiquitin E3 ligases, and prolyl isomerases. We describe a sequential and linear causality between post-translational modifications of RUNX2 by these enzymes. RUNX2 is one of the most important osteogenic transcription factors; however, it is not a suitable drug target. Here, we suggest enzymes that directly regulate the stability and/or transcriptional activity of RUNX2 at a post-translational level as effective drug targets for treating bone diseases.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.506-508
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• 1986

Metabolic activity of inorganic nitrogenous compounds affects not only microbial growth but also metabolite production in fermentation technology. We have worked on the enzymes participating in ammonia assimulation of some fermentation bacteria. This paper summarizes the results on glutamine synthetase and its application in practical field. Glutamine synthetase (L-glutamate:ammonia ligase, EC. 6.3.1.2) catalyzes the formation of glutamine from glutamate and ammonia at the expense of cleavage of ATP and inorganic phosphate. The enzyme plays a dual role in nitrogen metabolism in bacteria; it is a key enzyme not only in the biosynthesis of various compounds through glutamine but also in the regulation of synthesis of some enzymes involved in the metabolism of nitrogenous compounds. The detailed works with the Eschericia coli and other enterobacterial enzymes revealed that glutamine synthetase is controlled by the following complex of mechanisms: (a) feedback inhibition by end products, (b) repression and derepression of enzyme synthesis, (c) modulation of enzyme activity in response to divalent cation and (d) covalent modification of enzyme protein by adenylylation and its cascade control. Comparative studies have also been made on the enzymes from other organisms.

• Microbiology and Biotechnology Letters
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• v.50 no.2
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• pp.235-239
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• 2022

Psychrophiles have evolved to produce cold-adapted enzymes to enable survival in low-temperature environments. In this study, the cold adaptation of 5-enolpyruvylshikimate-3-phosphate synthase (CpsEPSPS) from Colwellia psychrerythraea, a model psychrophile, was analyzed. The optimum temperature for the activity of CpsEPSPS was found to be 25℃, with 35% activity remaining at 5℃. However, the unfolding temperature of CpsEPSPS was 54℃. This phenomenon is frequently observed in cold-active enzymes. As is the cases for most cold-active enzymes, the K_m values of CpsEPSPS for its substrates were higher than those of Escherichia coli EPSPS. These results indicate that CpsEPSPS is cold-adapted, but not perfectly.

• Molecular & Cellular Toxicology
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• v.4 no.4
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• pp.300-306
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• 2008

We investigated high light-induced alterations in antioxidant enzymes by exposing green vegetative cells of the alga Haematococcus pluvialis to excess irradiance to induce the production of astaxanthin, a carotenoid pigment. Total activity of catalase decreased approximately 70% after high light exposure, whereas glutathione peroxidase (GPX) activity was slightly enhanced. Total activity of superoxide dismutase and ascorbate peroxidase (APX) also slightly decreased. Overall, we did not observe dramatically elevated levels of antioxidant isozymes, although APXn, GPX2, and GPX3 isozyme increased slightly. ${H_2}{O_2}$ content increased about sixfold after high light exposure, demonstrating severe cellular oxidative stress, whereas lipid peroxidation was notably reduced. Concomitantly, astaxanthin accumulation increased about sevenfold. This result suggests that probably massively accumulated astaxanthin may be one of the antioxidant protector against high light stress.

• Biomedical Science Letters
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• v.12 no.4
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• pp.427-433
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• 2006

We investigated the effect of propolis on the activity of antioxidant enzymes in rat liver exposed by X-ray irradiation. The dosage of propolis showed the effect of lowering the concentration of superoxide anion in irradiated rat liver, suggesting that propolis has a significant role to remove superoxide anion as an antioxidant and/or by activating the antioxidant enzyme. The activities of superoxide dismutase (SOD) and glutathione reductase (GR), disturbed by X-ray irradiation, were restored in 30 days to normal status in the group which dosed propolis before X-ray irradiation. Interestingly, catalase (CAT) and glutathione peroxidase (GPOX) activities were highly increased with feeding propolis to rat compared to untreated group, whereas glutathione s-transferase (GST) activity was little affected. Taken together, it suggests that the propolis has a protective role in the rat liver cells against X-ray irradiation by increasing and recovering the activities of antioxidant enzymes.

• Korean Journal of Microbiology
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• v.19 no.3
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• pp.137-141
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• 1981

Occurrence and distribution of sucrose metabolizing enzymes in oral streptococci had been studied. In these studies, the carbohydrate component of the culture medium had been glucose. I have extended these studies by analyzing bacterial culture supernatants for the relative content of hexosyltransferases, namely glucosyl and fructosyltransferase. As a carbohydrate, fructose was used. The growth measured for nine oral streptococci (Strptococcus mutans strains BHT, ING, AHT, 6715, LM-7, and SL-1 ; Streptococcus sanguis 903, 9811, and M-5) varied. The level of glucosyltansferase activity also varied among S. mutans strains, and its level in S. sanguis was relatively low. Fructosyltansferase activity of the various strains fluctuated more than of glucosyltransferase. S.mutans strain LM-7 had significantly higher level of both enzymes. As a whole, fructose-grown cultures had generally an agreeable trend of enzyme activity to those from glucose-grown cultures.