• Food Science and Preservation
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• v.13 no.5
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• pp.563-568
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• 2006

The properties of mung bean were investigated depending on hydrolysis condition. The results showed that enzyme treatments (${\alpha}$-amylase and protease each at 0.1% (w/w)) by varying hydrolysis temperature showed better properties than non-pretense treatment (control group). The treatment with 0.08% ${\alpha}$-amylase was best for optimum hydrolysis of mung bean starch The treatment using a mixture of 0.08% (w/w) ${\alpha}$-amylase and 0.12% (w/w) protease was best for optimum hydrolysis of meg bean protein. The effects of Hydrolysis time of mung bean showed that the optimum time was 60 and 90 min and there fore the optimum time was set at 60 min. These result showed that the best hydrolysis conditions of mung bean were the treatment at $60^{\circ}C$ for 60 min using a mixture of 0.08%(w/w) ${\alpha}$-amylase and 0.12% (w/w) pretense, with the sugar level shown at $5.8^{\circ}Brix$, reducing sugar at 2,022.13 mg% and crude protein at 7,666.17 mg%.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.3
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• pp.509-514
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• 1994

Penicillium purpurogenum , which produces a copra galactomannan degrading enzyme extracellularyl, was isolated from soil , and its properties and formation condition of mannooligosaccharides were investigated. The optimum ph and temperature for the activity of the mannanase were 5.5 and 55$^{\circ}C$, respectively. The mannanase was stable in between pH 3.5 and 7.0 after 2 hr incubation at 3$0^{\circ}C$ lost 90% of the original activity after incubation at 55$\AA$ and pH 5.5 for 2 hr. With two different substrate concentration, hydrolysis of white coprameal proceeded rapidly at the early stage of the reaction, but gradually solwed thereafter especially at a higher concentration of copra meal (20 %). The enzyme hydrolyzed white copra meal to monosaccharides, mannobiose and mannotriose at the final stage of the reaction.

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.571-575
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• 2003

A marine aerobic Gram-negative bacterium, Pseudoalteromonas carrageenovora, has been blown to hydrolyze carrageenans, the sulfated galactans of red algae, and to desulfate oligo kappa-carrageenans. Recently, the gene encoding arylsulfatase (aryl-sulfate sulfohydrolase, E.C.3.1.6.1) of A. carrageenovora was cloned and the nucleotide sequence was reported. Enzymatic hydrolysis of sulfate groups in agaropectin simplifies the process of agarose preparation. In order to overproduce the enzyme, the arylsulfatase gene (astA, 984 bp ORF) from P. carrageenovora genome was amplified by PCR and subcloned into the pET21a vector. When the constructed plasmid pAST-A1 was introduced into E, coli BL21(DE3), the transformant on LB plate containing IPTG showed the hydrolyzing activity for p-nitrophenyl sulfate. Most of arylsulfatase activity was found in the cell lysate, but at $50\;{\sim}\;5000\;{\mu}M$ IPTG concentration the activity was found both in the culture supernatant and the cell lysate. The molecular weight of the recombinant enzyme was estimated to be 34 kDa by SDS-PAGE.

• Toxicological Research
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• v.23 no.1
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• pp.47-53
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• 2007

Amygdalin is a cyanogenic glycoside which is commonly found in almonds, bamboo shoots, and apri-cot kernels, and peach kernels. Amygdalin was first hydrolysed into prunasin, then degraded into cyanohydrin by sequential two-stage mechanism. The objective of this study was to examine the amygdalin decomposition and cyanide formation at various in vitro conditions, including acid, enzyme and anaerobic microbes (AM) in human feces (HF). In acid hydrolysis mimicking gastric environment, amygdalin was degraded to cyanide up to 0.2% in specific pH. In contrast, enzyme assay showed higher cyanide generation either by ${\beta}$-glucosidase, or by incubation with microbe. In conclusion, we are convinced of cyanide generation are occurred mainly by microbiological activities of the gut flora up to 41.53%. After ingestion with some staff, the degree and site of degradation in an organism is a key parst of regulatory decision making of that staff.

• Korean Journal of Microbiology
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• v.24 no.2
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• pp.119-126
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• 1986

A periplasmic endoprotease, named protease Pi, was purified to homogeneity from Escherkchia coli by conventional procedure with insulin as substrate. This enzyme degrades insulin and glucagon to trichloroacetic acid-soluble meterials, but shows little or no hydrolysis of bovine serum albumin, casein or globin. Its molecular weight was 110, 000 when determined by gel filtration on Sephacryl S-300 and was 105, 000 when estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Thus, it appears to be single polypeptide. This snzyme is metalloprotease, since it is completely inhibited by o-phenanthroline and can be activated by addition of divalent metal cations, such as $Mg^{2+}\;and\;Co^{2+}$. It is destinct from protease Ci, a cytoplasmic insulin degrading enzyme, since protease Pi is localized to the periplasm. Since protease Pi selectively degrades GTP cyclohydrolase I, it appears to play a role in the regulation of pteridine biosynthesis.

• Korean Journal of Microbiology
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• v.30 no.3
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• pp.213-217
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• 1992

Glucosyltransferase of Streptococcus mutans NCTC 10449 was purified and characterized. It relates with production of insoluble glucan in dental caries. The molecular weight was estimated to be 152.000. The optimum pH and temperature was 6.5 and $35^{\circ}C$. respectively. The enzyme was stable in alkaline pH. The Michaelis constants of the enzyme for releasing of fructose were 48 mM. Hydrolysis rate of insolut~le glucan by tlextranase was higher in S. mutuns NCTC 10449 than that of strains isolated from saliva.

• Applied Biological Chemistry
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• v.13 no.3
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• pp.223-229
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• 1970

1. The preparation and some enzymatic properties of crude alkaline protease from a thermophilic mold, Myriococcum sp. was investigated. 2. Optimum pH for the hydrolysis of casein was 9.0 at $50^{\circ}C$ for 10 minutes. Optimum temperature was $55^{\circ}C$ at pH 9.0 for 10 minutes. The enzyme was highly stable at the range of pH 6.0 to 11.0 at $30^{\circ}C$ 3. The alkaline protease in the culture filterate was isolated two fractions by elution column chromatography on DEAE-Cellulose.

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.250-255
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• 2005

Trichoderma inhamatum KSJ1, a filamentous fungus, isolated from rotten wood showed high ability to hydrolysis of cellulosic materials. Enzyme productivity by strain KSJ1 was high in the cultivation using carbon sources such as cellulosic materials and lignocellulosic wastes as rice straw and paper waste. In previous study peptone was one of optimum organic nitrogen sources in producing cellulases for saccharification of food wastes. However, it was too expensive using peptone as organic nitrogen source, so, in this study, soybean and yeast were applicated to substitute peptone. Yeast showed producing high enzyme activity, so it was estimated that yeast is available in producing cellulase using Trichoderma inhamatum KSJ1 at industrial Production.

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.260-265
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• 2005

In the previous research about ethanol production, we confirmed that SFW(saccharified foodwastes) medium(0.56g-ethanol/g-glucose) is mere efficient than YM medium(0.538g-ethanol/g-glucose). Ethanol production using SFW needs large enzyme cost due to the enzymatic hydrolysis of foodwastes, although the enzymes was obtained from our economical enzyme production methods, using the intact whole culture broth of Trichoderma harzianum FJ1. Therefore, in this research we used synchronous saccharification and fermentationmethod to produce ethanol using foodwastes. Ethanol production yield was 0.45g-ethanol/g-reducing sugar in synchronous saccharification and for-mentation by a fed-batch mode.

• Journal of Environmental Science International
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• v.14 no.10
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• pp.973-978
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• 2005

Biodegradable oil gelling agent was prepared, and their oil absorption capacities using light oil, lubricant oil and corn oil were investigated. The result showed that the oil absorption capacity was depended on the amount of surfactant and starch added, and was increased in the order of light oil, lubricant oil and corn oil. Also, the oil-absorption capacity was saturated within 30 min at $18^{\circ}C$. The biodegradability of the prepared biodegradable oil gelling agent was also studied by determination of reduced sugar produced after enzymatic hydrolysis. Their surface morphologies and thermal properties of the prepared biodegradable oil gelling agent were observed by scanning electron microscopy (SEM) and thermogravimetric analysis (TGA), respectively.