• Korean Journal of Food Science and Technology
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• v.32 no.3
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• pp.618-628
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• 2000

The indigestible dextrin I was prepared by hydrolyzing pyrodextrin with thermostable ${\alpha}-amylase$. The mean values of indigestible fraction and dieatry fiber of indigestible dextrin I prepared from yellow dextrin were 50.0% and 25.0%, respectively. Also the indigestible dextrin II was prepared by removing low molecular weight saccharides containing glucose with ethanol from enzyme hydrolysate of pyrodextrins. Over 80% of glucose and maltose in initial enzyme hydrolysate were removed, therefore the indigestible fraction and dietary fiber of the indigestible dextrins increased. The indigestible dextrin from ethanol precipitate of enzyme hydrolysate of yellow dextrin by ${\alpha}-amylase$ and amyloglucosidase showed a higher contents of indigestible fraction and dietary fiber than ethanol precipitates by any other enzyme combination, and its mean values were 83.6% and 62.8%, respectively. Consequently, it was found that the indigestible dextrins which are resistant to starch-hydrolysing enzyme can be easily prepared from pyrodextrin, and presumed that they can perform physiological functions as soluble dietary fiber.

• Korean Journal of Microbiology
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• v.31 no.1
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• pp.63-71
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• 1993

A xylanase (xylanase I) was purified 11.9-fold from the culture filtrate of Trichoderma koningii ATCC 26113 by the column chromatography on Sephadex G-75, SP-Sephadex C-50, DEAE-Sephadex A-50 and Sephadex G-50 with an overall yield of 8.2%. The molecular mass determined by gel filtration and sodium dodecyl sulfate polyacrylamide gel electrophoresis was found to be a monomeric polypeptide of ca. 35 kDa. The isoelectric point of the enzyme was estimated to be 9.3. The optimal reaction pH and temperature are 5.8 and 55.deg.C, respectively. The enzyme is stable up to 60.deg.C, while 78% of its activity is lost after the incubation for 10 min at 70.deg.C. The enzyme hydrolyzes sylan with relatively high activity, as well as carboxymethyl cellulose and avicel. The $K_{m}$ values of the enzyme for oat-spelf sylan, larchwood xylan and Avicel were 3.5, 1.6 and 10. 1 mg/ml, respectively. The enzyme hydrolyzed oat-spelt sylan to sylose, sylobiose, sylotriose and arabionoxylobiose, while it degraded larchwood xylan to xylose, xylobiose, xylotriose and arabionoxylobiose, while it degraded larchwood xylan to xylose, xylobiose and xylotriose as the major products. The hydrolysis patterns indicate that xylanase I is endo-enzyme.e.

• Microbiology and Biotechnology Letters
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• v.22 no.5
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• pp.485-490
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• 1994

A restriction endonuclease, PsyI, has been isolated from Pseudomonas syringae pv. pha- seolicola, and its catalytic properties have been studied. This enzyme was purified through strepto- mycin sulfate and ammonium sulfate fractionation, phosphocellulose Pll, DEAE-cellulose, hydroxy- apatite and Sephadex G-100 column chromatography. It's molecular weight was about 50,000 dalton as determined by 7.5% polyacrylamide gel electrophoresis containing 0.1% SDS. In catalytic proper- ties, PsyI shows stable at wide ranges of pH between 7.0 and 10.0, of temperature between 30$\circ$C and 37$\circ$C, and its thermal stability is between 25$\circ$C, and 45$\circ$C, at the presence Of 10 mM MgCl$_{2}$-PsyI essentially require Na salt for enzyme reaction, is rather inhibited in the high Na salt concent- ration. The presence of 2-mercaptoethanol is absolutely required for the enzyme activity. This endonuclease, PsyI was determined to be an isoschizomer of SalI from the results of the restriction mapping and DNA sequencing.

• Korean Journal of Microbiology
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• v.41 no.1
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• pp.81-86
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• 2005

One of the endoglucanases, F-I-III, was purified from the culture filtrate of T. sp. C-4 through procedures including chromatography on Sephacryl S-200, DEAE-Sepharose A-50, and Chromatofocusing on Mono-P (FPLC). The molecular weight of the enzyme was determined to be about 56,000 Da by SDS-PAGE, and pI of 4.9 by analytical isoelectric focusing. F-I-III showed the highest enzyme activity at $55^{\circ}C$, and the pH optimum of the enzyme was 5.0. There was no loss of activity when the enzyme was incubated at $50^{\circ}C$ for 24 hours. The specific activity of the enzyme F-I-III toward the CMC was 315.4 U/mg. The Km value for $PNPG_2$ of F-I-III was 2.69 mM. N-terminal sequence of F-I-III was analyzed to be QPGTSTPEVHPKKLTTYK. It showed $95\%$ of homology to that of EGI from T. reesei. The presence of some metal ions (1 mM) had only a little effect on CMCase activity. The treatment of the reducing agents resulted in the increase of endoglucanase activity.

• BMB Reports
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• v.35 no.3
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• pp.251-254
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• 2002

The genetic factors that contribute to the development of coronary artery disease (CAD) are poorly understood. It is likely that multiple genes that act independently or synergistically contribute to the development of CAD and the outcome. Recently, an insertion/deletion (I/D) polymorphism of the human angiotensin I-converting enzyme (ACE) gene, a major component of the renin-angiotensin system (RAS), was identified. The association of the ACE gene D allele with essential hypertension and CAD has been reported in the African-American, Chinese, and Japanese populations. However, other studies have failed to detect such an association. It has been suggested that these inconsistencies may be due to the difference in backgrounds of the population characteristics. In the present study, we investigated the I/D polymorphism of the ACE gene in 103 subjects of both sexes, consisting of 59 normal controls and 44 patients with hypertension. The allele and genotype frequency were significantly different between the hypertensive and control groups (p < 0.01). Among the three ACE I/D variants, the DD genotype was associated with the highest value of the mean systolic blood pressure [SBP] and mean diastolic blood pressure [DBP] (p = < 0.05) in men, but not in women. In the overall population, the mean SBP and DBP was highest in DD subjects, intermediate in I/D subjects, and the least in II subjects.

• Food Science of Animal Resources
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• v.43 no.6
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• pp.989-1001
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• 2023

Processed foods containing pork fat tissue to improve flavor and gain economic benefit may cause severe issues for Muslims, Jews, and vegetarians. This study aimed to develop an indirect enzyme-linked immunosorbent assay (iELISA) based on a monoclonal antibody specific to thermal stable-soluble protein in pork fat tissue and apply it to detect pork fat tissue in heat-processed (autoclave, steam, roast, and fry) beef meatballs. To develop a sensitive iELISA, the optimal sample pre-cooking time, coating conditions, primary and secondary dilution time, and various buffer systems were tested. The change in the iELISA sensitivity with different 96-well microtiter microplates was confirmed. The detection limit of iELISA performed with an appropriate microplate was 0.015% (w/w) pork fat in raw and heat-treated beef. No cross-reactions to other meats or fats were shown. These results mean that the iELISA can be used as an analytical method to detect trace amounts of pork fat mixed in beef.

• Environmental Analysis Health and Toxicology
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• v.17 no.3
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• pp.265-272
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• 2002

This study was carried out with the detection for multiresidue of the organophosphorus pesticides such as malathion, parathion. diazinon, and carbamate pesticide such as carbaryl, by enzyme-inhibition method. The acetylcholinesterase (AChE) and cholinesterase (ChE) activities in chicken brain determined by the Ellman's method were 166.6 and 5.8 $\mu$mol/min/g protein, and in chicken plasma were 23.1 and 8.3 $\mu$mol/min/g protein, respectively. The optimum pH of AChE and ChE was 8.2 and 7.8, respectively. The Km of AChE and ChE was 0.034 and 0.045 mM, respectively. I$\_$50/ for AChE and ChE by some organophosphorus was 55.82 and 99.42 mg/L of malathion, 31.16 and 29.13 mg/L of parathion, and 17.89 and 19.62 mg/L of diazinon, respectively. I$\_$50/ for AChE and ChE by carbaryl of carbamate was 0.10 and 0.05 mg/L, respectively. The 0.07 mg/L of drinking water advisory level for carbaryl could be detected with I$\_$50/ of AChE and ChE. Enzyme-Inhibition (EI) method with AChE and ChE was used the multiresidue method to detect the 1 mg/L of the carbamate pesticides.

• Journal of the Korean Institute of Electrical and Electronic Material Engineers
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• v.15 no.7
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• pp.615-620
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• 2002

In the case of immobilizing of glucose oxidase into polypyrrole (PPy) using electrosynthesis, the glucose oxidise (GOx) forms a coordinate bond with the polymers backbone. However, because of intrinsic insulation and net-chain of the enzyme, the charge transfer and mass transport are obstructed during the film growth. Therefore, the film growth is dull. We synthesized enzyme electrodes by electropolymerization added some organic solvent, such as ethanol and tetrahydrofuran (THF). The formative seeds of film growth was delayed by adding ethanol. The delay was induced by radical transfer between ethanol and pyrrole monomer. The radical transfer reactions shared the contribution of dopants between electrolyte anion and GOx polyanion. This led to increase amount of immobilized the enzyme in PPy. For the UV absorption spectra of synthetic solution before synthesis and after, in the case of ethanol added, the optical density was slightly decreased for the GOx peaks. It suggests amount of GOx in the solution was decreased and amount of GOx in the film was increased.

• Journal of Ginseng Research
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• v.19 no.3
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• pp.237-243
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• 1995

Agmatine iminohydrolase (EC 3.5.3.12) catalyzes the hydrolysis of agmatine into putrescine. The enzyme seems to be one of the critical enzymes in putrescine biosynthesis. The enzyme was purified to homogeneity from Panax ginseng C.A. Meyer by combined method of ammonium sulfate 1 fractionation, DEAR anion exchange column, hydroxyapatite column and agmatine carboxyhexyl Sepharose 4B affinity column. The molecular weight estimated by native pore gadient polyacrylamide gel electrophoresis was 71, 000 Dalton, while that estimated by SDS-PAGE was 70, 000 Dalton, indicating a monomeric enzyme. The optimal pH and temperature were 9.0 and 37$^{\circ}C$, respectively. The Km and 1 Vmax for agmatine were 8.3 mM and 14.4 nmole/hr, respectively. Heat stability of this enzyme was high. The enzyme was observed to be inhibited by polyamines such as putrescine, cadaverine, spermidine and spermine. Especially, putrescine was a potent inhibitor of the purified enzyme. These results suggest that polyamines could be important in growth regulation of Panax ginseng C.A. Meyer.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.180.1-180.1
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• 2003

Eukaryotic DNA topoisomerase I (top I) is an essential enzyme that act to relax supercoiled DNA during the transcription, replication and mitosis. Intracellular levels of top I are elevated in a number of human solid tumors, relative to the respective normal tissues, suggesting that controlling the topI level is important to treat cancer. Top I poisons show their antitumor activities by stabilizing the cleavable ternary complex consisting of top I enzyme, DNA, and drug. Thus, top I is a promising target for the development of new cancer chemotherapeutics against a number of solid tumors. (omitted)