• Korean Journal of Food Science and Technology
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• v.27 no.1
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• pp.74-79
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• 1995

Autoclaved juices of common vegetables including cabbage were growth inhibitory to various microorganisms. Sensitivity of microorganisms to antimicrobial action of autoclaved vegetable juices was different depending on microbial strains. Lactic acid bacteria and Gram negative bacteria were less sensitive while non-lactic Gram positive bacteria and yeasts were very much sensitive to antimicrobial action of autoclaved cabbage juice(ACJ). Staphylococcus aureus and Candida utilis whose growth were completely inhibited in ACJ could grow in ACJ diluted with distilled water. This suggests that microorganisms were not able to grow in ACJ because of growth inhibitory compounds produced during heating but not because of the lack of nutrients. Cabbage juice heated at $100^{\circ}C$ for up to 30 min was not inhibitory while that heated at $121^{\circ}C$ for 5 min was. Heating temperature was an important parameter in generating growth inhibitory compound in heated cabbage juice.

• Korean Journal of Food Science and Technology
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• v.27 no.6
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• pp.978-984
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• 1995

This study was conducted to investigate the physiological functionality of the hot water and 70% acetone extracts obtained from the pine needle and mugwort. Flavanol tannin content was above 60% of the total polyphenol in pine needle extracts. 70% Acetone extract from pine needle exhibited inhibition percentage of about 82.2% on the mutagenicity of Trp-P-1. Angiotensin I converting enzyme(ACE) inhibition activity was 61% and 50% in the hot water extract and in the 70% acetone extract respectively. Electron donating ability(EDA) of the hot water and 70% acetone extracts obtained from the pine needle was significantly good above 80%. 70% Acetone extract from pine needle showed inhibitary effect against the polyphenol oxidase(PPO) of water dropwort. The nitrite scavenging ability was appeared in all the extracts examined and it showed $80{\sim}90%$ at pH 3.0. The oxidative stability was determined by POV. Results showed that ethyl acetate fraction is better antioxidants than chloroform and butanol fractions in the soybean oil. Then, in the mugwort extracts, antimutagenicity of 70% acetone extract was similar to that of pine needle. Ratio of ACE inhibition activity was higher than that of pine needle extracts. EDA of hot water and 70% acetone extracts was 45%. Extracts from the mugwort were lower in nitrite scavenging ability about $20{\sim}30%$ than extracts from pine needle.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1977.10a
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• pp.195.4-196
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• 1977

Trypsin에 대해서 비해물질을 생성하는 Streptomyces속 균주 AS 707을 선별하고 이 균주가 생성하는 물질의 작용성 및 제성질을 조사한 결과 본 저해물질은 열에 대해서 비교적 강하고 pH 처리에 대해서는 산성에서 중성에 걸쳐서는 안정하나 alkali성에서는 불안정했고 $\alpha-chymotrypsin과$ papain에 대해서도 저해작용을 하였으며 trypsin에 대한 저해양상은 mixed type이었다.(중략)

• Korean Journal of Fisheries and Aquatic Sciences
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• v.25 no.3
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• pp.229-235
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• 1992

Fish protein hydrolysates(FPH) prepared from defatted mackerel meal by proteases such as complex enzymes, bromelain, alcalase, $\alpha-chymotrypsin,$ trypsin, papain and pepsin were tested for inhibitory activity against angiotensin-I converting enzyme(ACE). Among proteases tested, the hydrolysates obtained from the treatment of complex enzymes or bromelain showed relatively higher activity. ACE inhibitory activity of the hydrolysates increased until hydrolysis of 8 hrs, and was stable by heat treatment for 20min at $100^{\circ}C.$ From the profiles of fractionation of the hydrolysates with Bio-gel P-2, the most active fraction had about MW 1,450 and it's amino acid was abundant in Asp, Glu, Lys, Leu, Val and Ala. $IC_{50}\;(amounts\;of\;inhibitors\;needed\;for\;50\%\;inhibition)$ of the active fraction of the hydrolysates obtained from the treatment of complex enzyme and bromelain was 90 and $130 {\mu}g,$ respectively.

• Journal of the Korean Chemical Society
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• v.20 no.5
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• pp.406-416
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• 1976

A series of $N^1$-alkylnicotinamide chlorides, $N^1$-methyl-to $N^1$-dodecylnicotinamides inclusive were studied with rabbit muscle L-${\alpha}$-glycerophosphate dehydrogenase to investigate the possibility of reversible and irreversible inactivation of the pyridine-linked dehydrogenases by the coenzyme-competitive inhibitor derivatives. The inhibition of the enzyme by $N^1$-alkylnicotinamide chlorides was demonstrated to be reversible at the dilute concentration of the inhibitors but this reversible inhibition was found to be followed by an irreversible time-dependent inactivation measuable at high concentrations of the inhibitors. The properties of this time-dependent inactivation were discussed on the basis of the denaturation of the enzyme by the binding of small micelle-like structures formed at higher concentrations of the inhibitors.

• Journal of Food Hygiene and Safety
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• v.2 no.4
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• pp.181-189
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• 1987

To find esterase inhibitors and in the metabolites of Streptomyces strain DMC-498, two active compounds were isolated from the methanol extract of the mycelia of the strain by Silica gel column chromatography and preparatory argentation TLC. These compounds were proved to show competitive inhibition. Compound B was found to consist of linoleic and oleic acids. Fifty percent inhibition concentration ($lC_{50}$) of linoleic acid was $0.045\mu\textrm{g}/ml$, whereas oleic acid exhibited no inhibitory activity. Associated lipids: isostearic acid, isostearic acid methyl ester, oleic acid methyl ester and linoleic acid methyl ester, were isolated from the same extract, showing no inhibition of the esterase. Compound A was found to be a liquid inhibitor with an alicyclic ring and two or more oxygens, its molecular weight being more than 500.

• Proceedings of the Korean Nutrition Society Conference
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• 2001.05a
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• pp.196.1-196
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• 2001

• Microbiology and Biotechnology Letters
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• v.15 no.2
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• pp.129-134
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• 1987

Aspergillus sp. (MK-24) producing a biological active substance that inhibited the venom proteinase activity was isolated from soil. The substance also inhibited the activity of trypsin and coagulation of blood, but did not inhibit papain, $\alpha$-chymotrypsin and pepsin. The substance was partially purified from culture filtrate by precipitaion with acetone, and by chromatography of DEAE-Sepadex A-50 column and Amberlite IRC-50 ion exchange. The inhibitory substance was stable in the wide pH range from 2.0 to 12.0 at 37$^{\circ}C$, but not stable at $65^{\circ}C$ in the alkaline pH. Only 12% of the activity was decreased by the heat treatment at 10$0^{\circ}C$ for two hours. The inhibition on venom proteinase (Agkistrodon bromohoffi brevicaudus) was a mixed type. The inhibitory activity depended on the preincubation time and completely depressed by cupric, zinc and cobalt ions. The inhibition on the venom proteinase was appeared strongly on casein but not on ovalbumin or hemoglobin as a substrate.

• Microbiology and Biotechnology Letters
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• v.10 no.4
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• pp.283-288
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• 1982

Trypsin inhibitor produced by Streptomyces sp. was investigated its reactive characteristics against trypsin. The mode of inhibition against trypsin was mixed type of non-competitive and competitive with casein, and enzyme-inhibitor complex was formed rapidly. The inhibitory activity was increased by the addition of isoleucine and depressed by silver, mercuric or cupric ion. And when egg albumin or hemoglobin was used as substrate for trypsin, the inhibition ratio was changed. The inhibitor inhibited coagulation of blood of bovine.

• Journal of the Korean Society of Food Science and Nutrition
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• v.25 no.6
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• pp.1069-1073
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• 1996

Inhibition of xanthine oxidase by seaweed extracts obtained from Undaria pinnatifida, Ecklonia stolonifera, Ecklonia cava, Laminaria japonica, Sargassum, Codiumfragile, Enteromorpha compressa and Porphyra tenera were investigated. Extracts of E. stolonifera and E. mua remarkably inhibited xanthine oxidase activity compared to those of other seaweed. The xanthine oxidase inhibitory activity of E. cava was higher than that of E. stolonifera. Diethyl ether extract from E. cava was more effective in the inhibition of xanthine oxidase than other solvent extracts. Two xanthine oxidase inhibitors(A-1 and A-2) from diethyl ether extract were isolated and purified by silica gel column chromatography, thin layer chromatography and high performance liquid chromatography. Xanthine oxidase inhibitory activities of these compounds were 27.8 and 48.1% per 0.4mg, respectively. The active compound A-2 had absorption peak at 420nm, 456nm and 467nm, which can be considered as siphonaxanthine.