• Journal of Microbiology
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• v.41 no.1
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• pp.58-62
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• 2003

An extracellular pretense of Bacillus amyloliquefaciens S94 was purified to apparent homogeneity. The enzyme activity was strongly inhibited by general inhibitor for serine protease, PMSF, suggesting that the enzyme is a serine pretense. The purified enzyme activity was inhibited by leucine peptidase inhibitor, bestatin, suggesting that the enzyme is a leucine endopeptidase. The maximum proteolytic activity against different protein substrates occurred at pH 10, 45$^{\circ}C$ (protein substrate) and pH 8, 45$^{\circ}C$ (synthetic substrate). The purified enzyme was specific in that it readily hydrolyBed substrates with Leu or Lys residues at P$_1$ site. The pretense had characteristics of a cold-adapted protein, which was more active for the hydrolysis of synthetic substrate in the range of 15$^{\circ}C$ to 45$^{\circ}C$, specially at low temperature.

• Corrosion Science and Technology
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• v.8 no.5
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• pp.197-202
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• 2009

The high toxicity of wax, oil, varnish and volatile corrosion inhibitor(VCI) corrosion inhibitors lead to an increasing interest in using non-toxic alternatives such as anti-corrosive film. This study aims to investigate the possibility to use acryl based anti-corrosive film as a substitution of toxic corrosion inhibitors. Acryl emulsions were polymerized by several acryl monomers(acrylonitrile(AN), n-butyl acrylate(nBA), methylmethacrylate(MMA) and glycycyl methacrylate(GMA)), non-toxic corrosion inhibitor, crosslinking agents(diethylene glycol dimethacrylate(DEGDA)) and various additives in order to apply substrate of anti-corrosive film. Acryl emulsion for anti-corrosive film(AeACF) as a substrate of corrosion inhibitor film has excellent removal characteristic at above $25^{\circ}C$. The crosslinked by DEGDA in a range of above 4 wt% content anti-corrosive film can easily remove from the metal surface by using hands because it kept a balance of cohesion and adhesion strength. Anti - corrosive performance of AeACF is better than anti-corrosive oil by corrosion rate test, which was measured $54.3mg/dm^2$ day(MDD) and $142.9mg/dm^2$ day, respectively. Anti-corrosive film consisting of acryl monomers and inorganic anti-corrosive ingredients did not emit any toxic pollutants by gas chromatography. Thus it is estimated that acryl based anti-corrosion film can substitute toxic corrosion inhibitors.

• International Journal of Industrial Entomology and Biomaterials
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• v.1 no.1
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• pp.73-78
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• 2000

We investigated some biochemical properties of acetylcholinesterase (AChE) in the Bombyx mori larval head. 1% Triton X-100 (v/v) was suitable for extracting AChE from the silkworm larval head but 1 M NaCl was not suitable. PAGE analysis showed a single band of AChE that was detected by histochemical staining using acetylthiocholine as a substrate. AChE was also partially purified with Sepharose 6B and DEAE-cellulose column. Finally, the specific activity of partially purified enzyme solution was 7.6. The study on inhibitor specificity indicated that the enzyme under study was a true cholinesterase (ChE) or AChE. AChE activity was maximum at the substrate concentration of $5{\times}10^{-4}$ M and the excess substrate inhibited the AChE activity. The optimal pH and temperature were pH 7.0-9.0 and 30-35$^{\circ}C$.

• Journal of Microbiology and Biotechnology
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• v.21 no.6
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• pp.617-626
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• 2011

Transglutaminase from Streptomyces mobaraensis is an enzyme of unknown function that cross-links proteins to high molecular weight aggregates. Previously, we characterized two intrinsic transglutaminase substrates with inactivating activities against subtilisin and dispase. This report now describes a novel substrate that inhibits papain, bromelain, and trypsin. Papain was the most sensitive protease; thus, the protein was designated Streptomyces papain inhibitor (SPI). To avoid transglutaminase-mediated glutamine deamidation during culture, SPI was produced by Streptomyces mobaraensis at various growth temperatures. The best results were achieved by culturing for 30-50 h at $42^{\circ}C$, which yielded high SPI concentrations and negligibly small amounts of mature transglutaminase. Transglutaminasespecific biotinylation displayed largely unmodified glutamine and lysine residues. In contrast, purified SPI from the $28^{\circ}C$ culture lost the potential to be cross-linked, but exhibited higher inhibitory activity as indicated by a significantly lower $K_i$ (60 nM vs. 140 nM). Despite similarities in molecular mass (12 kDa) and high thermostability, SPI exhibits clear differences in comparison with all members of the wellknown family of Streptomyces subtilisin inhibitors. The neutral protein (pI of 7.3) shares sequence homology with a putative protein from Streptomyces lavendulae, whose conformation is most likely stabilized by two disulfide bridges. However, cysteine residues are not localized in the typical regions of subtilisin inhibitors. SPI and the formerly characterized dispase-inactivating substrate are unique proteins of distinct Streptomycetes such as Streptomyces mobaraensis. Along with the subtilisin inhibitory protein, they could play a crucial role in the defense of vulnerable protein layers that are solidified by transglutaminase.

• Journal of Microbiology and Biotechnology
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• v.7 no.5
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• pp.333-340
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• 1997

An actinomycetes, KT-10 isolated from ginseng field in Kyongpook, Korea was selected based on its ability to produce a lysosomal cathepsin B inhibitor. The inhibitor purified from the culture supernatant of the isolate KT-10 showed strong inhibitory effects against cathepsin B as well as against papain when the activities were measured using synthetic substrate, ${\alpha}$-N-benzyloxycarbonyl-L-Iysine p-nitrophenyl ester (CLN) or ${\alpha}$-N-benzoyl-D,L-arginine 2-naphthylamide (BANA). The isolate KT-10 was identified as a species of Streptomyces based on its morphological characteristics and chemotaxonomic data. The TAXON program of Ward was used to identify Streptomyces sp. KT-10 as a strain of Streptomyces luteogriseus belong to cluster 18 of the genus Streptomyces with a Willcox probability 0.999388. The cathepsin B inhibitor was presumed to a novel material composed of a polyhydroxylamine.

• Microbiology and Biotechnology Letters
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• v.18 no.5
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• pp.501-505
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• 1990

Streptomyces sp. KISl3 isolated from soil was found to produce low molecular weight thiol protease inhibitors. The protease inhibitor production was closely linked to the cell growth and regulated by growth condition. The inhibitor was purified from the culture broth through butanol extraction, silicagel 60 column chromatography, Sephadex LH-20 gel filtration and preparative HPLC. The inhibitor showed specific inhibitory activity to thiol protease such as papain, picin and bromelain. The mode of inhibition against papain to Hammersten casein as a substrate was non-competitive.

• The Korean Journal of Food And Nutrition
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• v.11 no.6
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• pp.673-677
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• 1998

A inhibitor acting on substrate proteolytic enzyme was isolated from culture broth of Streptomyces sp. SK-862, which had been isolated from soil in Wonju City, by using the colloidal agar medium. The optimum culture temperature and initial pH for the production of the protease inhibitor was 28$^{\circ}C$ and pH 8.5, respectively. The optimum culture medium was composed of 1.5% glucose, 0.5% peptone, 0.1% K2PHO4, 0.05% CaCO3 and initial pH 8.5. The inhibitor production was maximum when the strain was incubated in shaking incubator at 70 strokes for 60 hours.

• Journal of the Korean institute of surface engineering
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• v.29 no.2
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• pp.100-108
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• 1996

The internal stress of acidic electroless nickel deposits on zincated aluminum was determined by spiral contractometer. Several plating conditions such as inhibitor and complexing agent concentrations and pH affecting the internal stress were studied. The resulting intrinsic stress contribution to the total stress was discussed in terms of phosphorous content of the deposit, solution pH, and surface morphology. However, the most important was found to be thermal stress for the total stress of Al substrate, because of high thermal expansion coefficient of the aluminum 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 institute of surface engineering
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• v.27 no.2
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• pp.109-117
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• 1994

Effect of ultrasonic agitation on the contact properties was studied in Ni electroless plating and Pd activation. P-type Si bare wafers were used as substrate and DMAB was used as reducing agent due to its good electrical properties, solderability and compatibility to substrate. In activation, high density Pd nuclei of small size were formed during ultra-sonic agitation compared to that of no stirring. In electroless plating, the plating rate was enhanced by 30∼90% by using ultrasonic agitation. In elecrtoless plating, inhibitor is the most effective additives in ultrasonic agitation. In this experi-ment, thiourea was used as inhibitor. The less the amount of the inhibitor, the more ultrasonic agitation efficiency. It is confirmed by SEM that Ni-B films formed by ultrasonic were coarser, less porous, and denser than those of no stirring. In ultrasonic agitation, boron content of the films was more than those of no stirring. In this case, the more DMAB concentration, the higher the temperature, the less pH, the more boron content. Resistivity of the films formed by ultrasonic agitation was higher than that of no strirring. As the content of boron was increased, the resistivity of the films was increased exponentially.