• Microbiology and Biotechnology Letters
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• v.19 no.2
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• pp.122-127
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• 1991

A bacterial strain NO. 32 which produced thermostable ${\alpha}$-amylase was isolated from soil and identified to genus of Bacillus. To enhance ${\alpha}$-amylase productivity, a successive mutation of Bacillus sp. No. 32 was attempted with treatment of N-methyl-N'-nitro-N-nitrosoguanidine (NTG). The resulting mutant, Bacillus sp. No. 32H417, which is risistant to refampicin and deficient in spore formation, produced about 90-fold high level of ${\alpha}$-amylase when compared with parental strain. The properties of the enzyme for thermostability were investigated. The optimal temperature and pH for enzyme reaction were 95$^{\circ}C$ and pH6.5, respectively, in the presence of 0.3mM $Ca^{2+}$ as an effective stabilizer.

• YAKHAK HOEJI
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• v.5 no.1
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• pp.45-50
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• 1960

Some enzymatic properties of Cynthia roretzi v. (Drasche Korean : U-Rung-Shei) was studied by author and obtained the following results; 1. The optimum pH of the digestive gland amylase was 6.8-7.0 2. Activity of metallic ion on the amylase showed the following order; 10$^{-3}$ M M $n^{++}$>10$^{-3}$ M $Co^{++}$>10$^{-4}$ M $Mg^{++}$>10$^{-4}$ M $Ca^{++}$>10$^{-2}$ M Z $n^{++}$>10$^{-2}$ M P $b^{++}$ 3. The digestive gland enzyme inactivated at 70.deg. C. 4. When the enzyme concentration increase 2 times, the enzymatic activity also increase, but not propertionally. 5. The digestine gland amylase showed remarkably higher enzymatic activity than the intestinal amylase. 6. The digestive gland amylase from the ascidian showed remarkably higher enzymatic activity than the heptancreatic amylase from shell fish (Turbo (Batillus) Cornutus Solander).nder).nder).

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.9
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• pp.1273-1279
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• 2006

The quality properties of oak mushroom were investigated using extraction conditions and enzyme treatments. The physiochemical properties were excellent at the extraction temperatures of $20^{\circ}C\;and\;40^{\circ}C$. The quality was increased as the extraction time increased but was best at the extraction time of 10 hr. The physiochemical properties such as soluble solid, reducing sugar and crude protein contents were best at the solvent ratio of 1:100 (w/v) so that it was set at 1:100. Thus, enzyme treatment was done at $50^{\circ}C$ for 2 hr with the solvent ratio of 1:100. The result showed that the best quality was shown using 0.2% protease and 0.2% cellulase. With the enzyme treatment, the essential amino acid contents increased by two folds but no difference was shown in $\beta-glucan$ content.

• Journal of environmental and Sanitary engineering
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• v.5 no.2
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• pp.103-110
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• 1990

For production of thermophilic and alkaline protease, Bacillus sp. strain AP-5 was isolated from a compost. The production of the protease was reached at maximum for 4 days at $55^{\circ}$ in standing culture. Chitin and Cellulose as carbon source, and Skim Milk as nitrogen source were favorable for the production of the enzyme. Optimal temperature and optimal pH of the enzyme was $55^{\circ}$ and 11, respectively. Metal ion didn't effect on the enzyme activity, the protease was very stable at heat treatment of 30 min at $55^{\circ}$.

• KSBB Journal
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• v.14 no.4
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• pp.470-475
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• 1999

Several enzyme were applied to Laubholz Bleached Kraft Pulp(LBKP) to evaluate the influence on beatability which was measured in Schopper Riegler value, and the results were compared with untreated pulp. Among the types of enzyme, cellulase was found to be the most effective. Addition of cellulase increased the beatability by 28% at optimum condition. Strength properties such as tensile strength and folding endurance also increased with enzymatic treatment by 12% and 46%, respectively. However, excessive dosage of cellulase had an adverse effect on strength properties in spite of the high beatability. Fibrillization by cellulase and destruction of fiber by excessive reaction was observed by Scanning Electron Microscopy(SEM).

• Fisheries and Aquatic Sciences
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• v.1 no.2
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• pp.209-215
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• 1998

Trypsin-like enzyme was purified from shrimp hepatopancreas through Q-Sepharose ionic exchange, benzamidine Sepharose-6B affinity, and Superdex 75 gel chromatography. Purity of trypsin-like enzyme was increased 69-fold with $44\%$ yield. The enzyme consisted of a single polypeptide chain with a molecular weight (M.W.) of 32 kDa judged by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme was completely inactivated by serine enzyme inhibitors such as soybean trypsin inhibitor (SBTI), tosyl-L­lysine chloromethyl ketone (TLCK), and leupeptin. However, the enzyme was not affected by tosyl-L-phenylalanine chloromethyl ketone (TPCK) which is a chymotrypsin specific inhibitor. The enzyme had no activity against benzoyl-tyrosine ethyl ester (BTEE) which is a chymotrypsin specific substrate. The enzyme showed high activity on the carboxyl terminal of Phe, Tyr. Glu, Arg, and Asp. However. no activity was detected against the carboxyl terminal of Pro, Trp, Cys, Gly, Val, and Ala.

• Journal of Microbiology and Biotechnology
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• v.10 no.1
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• pp.35-42
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• 2000

Reaction characteristics of 4-methylcatechol 2,3-dioxygenase (4MC230) purified from Pseudomonas putida SU10 with a higher activity toward 4-methylcatechol than catechol or 3-cethylcatechol were studied by altering their physical and chemical properties. The enzyme exhibited a maximum activity at pH 7.5 and approximately 40% at pH 6.0 for 4-methylcatechol hydrolysis. The optimum temperature for the enzyme was around $35^{\circ}C$, since the enzyme was unstable at higher temperature. Acetone(10%) stabilized the 4MC230. The effects of solvent and other chemicals (inactivator or reactivator) for the reactivation of the 4MC230 were also investigated. Silver nitrate and hydrogen peroxid severely deactivated the enzyme and the deactivation by hydrogen peroxide severely deactivated the enzyme and the deactivation by hydrogen peroxide was mainly due to the oxidation of ferrous ion to ferric ion. Some solvents acted as an activator and protector for the enzyme from deactivation by hydrogen peroxide. Ascorbate, cysteine, or ferrous ion reactivated the deactivated enzyme by hydrogen peroxide. The addition of ferrous ion together with a reducing agent fully recovered the enzyme activity and increased its activity abut 2 times.

• The Korean Journal of Food And Nutrition
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• v.23 no.2
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• pp.171-177
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• 2010

The catabolic threonine dehydratase from Serratia marcescens ATCC 25419 was purified to homogeniety using Sephadex G-200 gel filtration and AMP-Sepharose 4B affinity chromatography. The molecular weight of the native enzyme was 120,000 by native pore gradient PAGE. The enzyme was composed of four identical subunits with subunit molecular weights of 30,000 by SDS-PAGE. The Km values of the enzyme for L-threonine with and without AMP were 7.3 and 92 mM, respectively. There were 2 moles of pyridoxal phosphate and 16 moles of free -SH groups per 1 mole of enzyme. The enzyme was inhibited by $\alpha$-ketobutyrate, pyruvate, glyoxylate, and phosphoenol pyruvate(PEP) in the presence of AMP, yet stimulated by cAMP and ADP. For enzyme properties in comparison with S. marcescens, E. coli, and S. typhimurium enzyme, such as the PLP content, number of free sulfhydryl groups, and existence of ADP binding site, the S. marcescens enzyme was more similar to the S. typhimurium enzyme than the E. coli enzyme. Of the three enteric bacteria, the E. coli and S. typhimurium enzyme was increased the activity by ADP and cAMP, respectively, but only the S. marcescens enzyme was increased the activity by both ADP and cAMP. Therefore, the subtle differences in the properties between enzymes from the three enteric bacteria may represent minor structural differences among these enzymes and warrants further study.

• Korean Journal of Microbiology
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• v.26 no.4
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• pp.324-331
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• 1988

Ascorbate oxidizing enzyme from the crude extract of Pleurotus ostreatus was purified by ammonium sulfate precipitation, preparative polyacrylamide gel electrophoresis, DEAE Sepharose CL-6B ion exchange chromatography and Sephadex G-150 gel filtration chromatography. The molecular weight of the enzyme estimated by Sephadex G-150 gel filtration chromatography was 140,000 and that of its subunit by SDS-polyacrylamide gel electrophoresis 66,000. The optimum pH for the maximum activity of the enzyme was 5.2 and the isoelectric point of the enzyme was 6.0 Km values for L-ascorbic acid and D-isoascorbic acid were both 2.2.$\mu$M, which indicates that the enzyme has the asme affinity towards both substrates.

• Korean Journal of Microbiology
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• v.27 no.3
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• pp.237-244
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• 1989

A soluble intracellular protease from cells of Pseudomonas carboxydovorans, a carboxydobacterium, grown on nutrient broth was purified 68-fold in five steps to better than 95% homogeneity with a yield of 2.4% using azocasein as a substrate. The enzyme activity was not detected from cells grown on pyruvate, succinate, acetate, or CO as a sole source of carbon and energy. The molecular weight of the native enzyme was determined to be 53,000. Sodium dodecyl sulfate-gel electrophoresis revealed the purified enzyme a monomer. The enzyme was found to be a serine-type protease. The enzyme activity was inhibited completely by several divalent cations such as $Cd^{2+}, Cu^{2+}, Hg^{2+}$, and $Fe^{2+}$. The enzyme was also inhibited by EGTA, but was stimulated by iodoacetamide. The optimal pH and temperature for the enzyme reaction were found to be 8.0 and $50^{\circ}C$, respectively. The enzyme was inactive on CO dehydrogenase.