• The Korean Journal of Pharmacology
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• v.32 no.3
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• pp.425-431
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• 1996

Human neutrophil elastases (HNElastase, EC 3.4.21.37), a causative factor of inflammatory diseases, are regulated by plasma proteinase inhibitors, alpha-proteinase inhibitor and ${\alpha}_2-macroglobulin$. Under certain pathological conditions, however, released enzymes or abnormal function of inhibitors may cause various inflammatory disease. NSAIDs have been clinically applied for treatment of inflammatory diseases. Inhibition of cyclooxygenase is a known mechanism of action of NSAIDs in the treatment of inflammatory disease. In in vitro experiments, HNElastase was inhibited by naproxen, phenylbutazone, and oxyphenbutazone, but ibuprofen, ketoprofen, aspirin, salicylic acid, and tolmetin did not inhibit elastase. HNElastase was also inhibited by chelating agents, EDTA & EGTA, and tetracyclines. Removal of divalent metal ions by EDTA caused inhibition of elastase, and reconstitution of the metal ions recovered the enzyme activity to a certain level. Frequencies and contours in the Raman spectra of various conditions of human neutrophil elastase undergo drastic changes upon partial removal and/or reconstitution of calcium and zinc ions. The metal ion content dependent activities and change of the contour of the Raman spectrogram suggest us that the mechanism of action of a chelator or chelator-like agents on neutrophil elastase may be related to the conformational change at/or near the active site, especially -C=O radical or -COOH radical.

• Microbiology and Biotechnology Letters
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• v.41 no.1
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• pp.119-127
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• 2013

Twenty-three strains of Leuconostoc species and 45 strains of Weissella species inhibiting the growth of Lactobacillus sakei, one of the most populous lactic acid bacteria in over-ripened kimchi, were isolated from kimchi in our previous study. Among these hetero-fermentative 68 strains, Leuconostoc mesenteroides CK0128, Weissella cibaria CK0633, and W. cibaria KK0797 exhibited a relatively high survival rate in MRS medium, which was adjusted to pH 4.3 using an acid mixture consisting of acetic and lactic acids, and produced a large amount of exopolysaccharides. The culture supernatants of 3 strains were fractionated by a molecular weight cutter and lyophilized. The fractions with a molecular weight smaller than 3,000 Da showed antagonistic activity against Staphylococcus aureus and Lb. sakei. The anti-bacterial substances were very stable to heat treatments ($121^{\circ}C$, 15 min) and active at acidic conditions below pH 5. ${\alpha}$-Amylase, lipase, and proteolytic enzymes (proteinase K and pepsin) did not affect their activities. These non-proteinaceous anti-bacterial substances inhibited the growth of several food pathogens.

• Korean Journal of Microbiology
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• v.42 no.4
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• pp.257-264
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• 2006

Fifty eight Cryptococcus neoformans strains isolated from clinical and environmental sources in Korea were examined for their serotypes and extracellular enzyme activities. Among the 51 strains isolated from clinical sources, 48 strains were serotype A (94.1%), 2 strains were serotype B (3.92%), and 1 strain was serotype D (1.96%). All seven environmental strains isolated from pigeon excreta were identified as serotype A. All isolates of C. neoformtans were positive for the production of extracellular proteinase and phospholipase. In the API-ZYM system, all fifty eight isolates produced alkaine phosphatase, esterase C4, esterase lipase: C8, leucine arylamidase, acid phosphatase, naphthol-AS-BI-phosphohydrase, $\alpha$-glucosidase and $\beta$-glucosidase. Thirty nine isolates (67.2%) of C. neoformans produced N-acetyl-$\beta$-glucosidase. Two isolates, serotype B, and B only one serotype A produced $\beta$-glucuronidase. Analysis of enzymatic profiles to 21 enzymes revealed four biotypic patterns among the 58 strains. The enzymatic patterns of C. neoformans isolated from clinical and environmental sources represented a significant relationship with the serotypes.

• Korean Journal of Food Science and Technology
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• v.7 no.4
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• pp.221-228
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• 1975

Meat tenderness is one of the most important factors in meat products because it plays a major role in the palatability of meat. To get information on the role of commercial meat tenderizer, the tenderizing ability of commercial meat tenderizer was measured with various substrates. The results obtained are as follows. 1. Content of crude protein in a commercial meat tenderizer was 4.9%. 2. Optimum temperature for proteolytic activity of meat tenderizer was $60{\sim}70^{\circ}C$. 3. Maximal activity of proteinase was obtained at pH $6{\sim}7$. 4. Proteolytic enzyme was activated by KCN, NaCN, EDTA. Thus, it was concluded that protease system of commercial meat tenderizer composed of plant origin proteinases. 5. Proteinase activity was completely inhibited by 10mM of N-Ethylmaleimide. 6. Commercial meat tenderizer showed stronger proteolytic activity on casein than on the water soluble fraction of meat protein, whereas it hydrolyzed the myofibrillar protein less efficiently.

• Asian-Australasian Journal of Animal Sciences
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• v.11 no.4
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• pp.375-380
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• 1998

Six Holstein heifer calves weaned at 45 days-of-age were randomly allocated into high daily gain (1.1 kg/d, HDG) and low daily gain (0.56 kg/d, LDG) groups, and were slaughtered at 170 kg of live weight. Energy intake level in the feeding period was 2.4 $\times$ maintenance in 105 days for HDG and 1.4 $\times$ maintenance in 216 days for LDG calves. Total length of the small intestine was identical between groups, but both weights of the pancreas and of the small intestinal mucosa were greater (p < 0.01) for HDG calves. Alpha-amylase, lipase, proteinase, and trypsin activities of the whole pancreas were higher (p < 0.05) in HDG calves. Disaccharidase activity of the whole small intestinal mucosa was also higher (p < 0.10) for HDG than for LDG calves. However, the enzymatic activities, expressed as per gram or per protein of the pancreas and the small intestinal mucosa, were not affected (p > 0.10) by the plane of nutrition. These results suggest that the digestive enzyme activity in the small intestine varies primarily with the weight of tissues synthesizing the enzyme.

• Food Science of Animal Resources
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• v.38 no.5
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• pp.1008-1018
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• 2018

Although bacteriocins with anti-listerial activity have been isolated from a wide variety of lactic acid bacteria, little is known about those from Leuconostoc lactis, a heterofermentative bacterium that produces diacetyl and exopolysaccharides in dairy foods. In this study, an anti-listerial bacteriocin was isolated from Leuc. lactis SD501 and characterized. It was particularly potent against Listeria monocytogenes and also inhibited Enterococcus faecalis. Anti-listerial activity reached a maximum during the early stationary phase and then decreased gradually. The anti-listerial substance was sensitive to proteinase K and ${\alpha}$-chymotrypsin, confirming its proteinaceous nature. Its activity remained stable at pH values ranging from 1 to 10. In addition, it was strongly resistant to high temperatures, retaining its activity even after incubation for 15 min at $121^{\circ}C$. The apparent molecular mass of the partially purified anti-listerial bacteriocin was approximately 7 kDa. The characteristics of the SD501 bacteriocin, including its small molecular size (<10 kDa), strong anti-listerial activity, wide pH stability and good thermostability, indicate its classification as a Class IIa bacteriocin.

• Korean Journal of Environmental Biology
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• v.22 no.4
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• pp.487-493
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• 2004

To investigate the antifungal activity related protein in pesticidal bacteria, a bacterial strain LTD was isolated from soil collected at Gimje in Jeonbuk province, Korea, and identified as Bacillus subtilis LTD based on a API50 CHB kit and 168 rDNA sequencing. It has an antifungal activity against 9 plant pathogenic fungi in a paper disc assay. The antifungal activity- deficient mutant, B. subtilis mLTD was induced at a 5 kGy dose of $^{60}Co$ gamma radiation. Using the two-dimensional electrophoresis and the matrix assisted laser desorption ionization time-of-flight mass spectrometry, the comparison analysis of proteins between the wild and mutant were performed. A major intracellular serine proteinase IspA (MW: 32.5 kDa), a NAD (P) H dehydrogenase (MW: 20.0 kDa), and a stage II sporulation protein AA, SpoIIAA (MW: 14.3kDa) were detected only in the B. subtilis LTD. These results suggested that the functions of these proteins found only in the B. subtilis LTD could. be closely related to the antifungal activity against plant pathogenic fungi.

• The Korean Journal of Physiology and Pharmacology
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• v.14 no.2
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• pp.71-75
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• 2010

To investigate the intestinal absorption of a fibrinolytic and proteolytic lumbrokinase extracted from Eisenia andrei, we used rat everted gut sacs and an in situ closed-loop recirculation method. We extracted lumbrokinase from Eisenia andrei, and then raised polyclonal antibody against lumbrokinase. Fibrinolytic activity and proteolytic activity in the serosal side of rat everted gut sacs incubated with lumbrokinase showed dose- and time-dependent patterns. Immunological results obtained by western blotting serosal side solution using rat everted gut sacs method showed that lumbrokinase proteins between 33.6 and 54.7 kDa are absorbed mostly by the intestinal epithelium. Furthermore, MALDI- TOF mass spectrometric analysis of plasma fractions obtained by in situ recirculation method confirmed that lumbrokinase F1 is absorbed into blood. These results support the notion that lumbrokinase can be absorbed from mucosal lumen into blood by oral administration.

• Journal of Microbiology and Biotechnology
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• v.10 no.2
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• pp.195-200
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• 2000

Bacillus cereus BS229 was identified as a bacteriocin producer with a bactericidal activity against Bacillus thuringiensis subsp. Thomsoni BR-40. Bacillus cereus BS229 and cerein BS229, named tentatively as the bacteriocin produced by Bacillus cereus BS229, showed a narrow spectrum of actibity against Gram-positive and Gram-negative bacteria, along with yeast and molds. Production of cerein BS229 in a 5-1 fermenter followed typical kinetics of primary metabolite synthesis. The antibacterial activity of cerein BS229 on sensitive indicator cells disappeared completely by ${\alpha}-chmotrypsin$ or proteinase K, which indicates its proteinaceous nature. Cerein BS229 seemed to be very stable throughout the pH range of 2.0 of 9.0 and it was relatively heat labile, despite the fact that bacteriocin activity was still detected after being boied for 30min. Cerein BS229 actibity has been changed with some of the organic solvents such as toluene, ethanol, and chloroform. Direct detection of cerein BS229 actibity on SDS-PAGE suggested that it had an apparent molecular mass of about 8.2 kDa.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.19 no.5
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• pp.469-476
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• 1986

Proteolytic activity of the tissue extracts from the muscle of mackerel, Scomber japonicus, and sardine, Sardinops melanostcta, was comparence with referenced to the optimum reaction condition. Thermal stability and change of proteolytic activity of the tissue extracts during storage were investigated. The existence of acid, weak acid and alkaline proteinase was identified in the ordinary and dark muscle of the mackerel and sardine. Specific activity of acid proteinase was stronger than weak acid or alkaline proteinase in the both fish. The proteolytic activity of the tissue extracts on the optimum reaction condition was: ordinary muscle of mackerel, 0.12 nM-Tyr. eq./mg-prot. /min. at pH 3.0 and $50^{\circ}C$; dark muscle of mackerel, 0.36 nM-Tyr. eq./mg-prot. /min. at pH 3.0 and $45^{\circ}C$; ordinary muscle of sardine, 0.45 nM-Tyr. eq./mg-prot. /min. at pH 2.4 and $45^{\circ}C$; dark muscle of sardine, 0.24 nM-Tyr. eq./mg-port. /min. at pH 2.4 and $45^{\circ}C$. The proteinases distributed in the muscle of mackerel and sardine were stable with the heat treatment at $45^{\circ}C$ for 5 minutes, but those in the dark muscle of mackerel was stable with the treatment at $5^{\circ}C$ for 5 minutes. The proteinases from the muscle were slowly inactivated with the whole storage days at $5^{\circ}C\;and\;-15^{\circ}C$, those were more stable at $-15^{\circ}C\;than\;5^{\circ}C$ storage.