• KSBB Journal
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• v.7 no.1
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• pp.79-83
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• 1992

The characteristics of Erwinia rhapontici cells with $\alpha$-glucosyltransferase activity immobilized in Ca-alginate beads and the performance of two different types of reactor-stirred tank reactor(STR) and packed bed reactor(PBR)-charged with these immobilized cells to produce palatinose from sucrose were investigated. The optimal pH(5.5-6.0) and temperature($30-35^{\circ}C$) showed no appreciable difference between free and immobilized cells. The apparent Km value of the immobilized cells(0.28M) was approximately two times higher than that of free cells(0.13M) at $30^{\circ}C$. The half life of the immobilized cells was found to be 380 h with STR while much greater operational stability was achieved with PBR. Continuous operation of PBR at a space velocity of $0.2h^{-1}$ for 30 days showed only 5% loss of initial activity.

• Journal of the Korean Society of Food Culture
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• v.5 no.2
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• pp.269-274
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• 1990

This study was conducted to determine invertase activity in persimmon during the drying process and characterize the purified enzyme. As drying proceeded, invertase activity increased until 10 days and decreased gradually afterwards. Invertase in persimmon fruit was extracted with 250 mM potassium phosphate sulfate buffer at pH 7.4. The enzyme was purified by means of ammonium sulfate fractionation, column chromatography on DEAE-cellulose and gel filtration on Sephadex G-200 column. The optimal temperature of enzyme was $40^{\circ}C$ and optimal pH was 5.0 and 6.0 for sucrose and raffinose, respectively. The enzyme was stable up to $50^{\circ}C$ and pH 3-6. The Km value of the enzyme, with sucrose as a substrate, was 2.5mM. Electrophoretic pattern of purified enzyme solution showed a single band.

• Microbiology and Biotechnology Letters
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• v.6 no.1
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• pp.1-8
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• 1978

In order to develop the processes for the production of fermented feed from cellulosic agricultural by-product, cereal straw, by th action of cellulolytic fungus, the properties of the cellulolytic enzyme produced by Trichoderma sp. KI 7-2 was studied. A higher enzyme activity was obtained in the culture added by 1％ rice or barley straw powder than in the culture of pure cellulose. The crude enzyme was prepared by precipitating from 20∼60％ saturated ammonium sulphate of the culture supernatant. The optimum conditions for the enzyme reaction were temperature of of 50$^{\circ}C$ and pH 4.2. The crude enzyme was static at 50$^{\circ}C$ for two hours and at pH between 4 and 6. These properties were adopted for the fermented feed production, and several production. Thus, several processes of semisolid culture were devicced to up grade tile fermented feed and to develop into the acceptable quality.

• Applied Biological Chemistry
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• v.13 no.3
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• pp.193-195
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• 1970

The cultural conditions of the osmophilic yeasts for higher concentration of NaCl selected in the previous report were examined and the results obtained were as follows. 1) The strain $T_3\;and\;T_8$ were grown exceedingly well on the media containing 15 percent of NaCl and $T_5\;and\;T_9,\;T_{10}\;and\;T_{11}$ on the media containing 5 percent of NaCl. 2) The optimum temperature for growth of the strain $T_3\;and\;T_5$ was $30^{\circ}C,\;T_8\;T_{10}$ and $T_{11}\;was\;25^{\circ}C\;and\;T_9\;was\;35^{\circ}C.$ 3) Their lethal temperature was $60^{\circ}C$ (treatment for 10 minutes). 4) The optimum pH for growth of the strain $T_3\;and\;T_8$ was pH 4.0, $T_5$ was pH 6.0 and $T_9\;T_9\;and\;T_{11}$ was pH 5.0, respectively.

• Korean journal of food and cookery science
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• v.13 no.5
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• pp.623-626
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• 1997

The purpose of this study was to investigate the properties of proteolytic enzymes extracted from mulberry (Morus alba L.). The protease activity of the enzymes from mulberry was 2,358 unit/g. The enzymes showed strong activities toward hemoglobin and collagen. The optimum temperature and pH of the enzymes were 50$^{\circ}C$ and 6.0, respectively. The enzymes were stable at the temperature range of 30$^{\circ}C$ to 60$^{\circ}C$ and the pH from 5.0 to 7.0 for 1 hr at 37$^{\circ}C$ of incubation and also retained whole activity after incubation for 1 hr at 60$^{\circ}C$.

• Applied Biological Chemistry
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• v.41 no.5
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• pp.349-354
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• 1998

The protease produced by Bacillus subtilis YG-95 was purified by precipitating with ammonium sulfate, DEAE-sepharose 6B and Sephadex G-100 column chromatogtaphies and its purified enzymological characteritics were investigated. The molecular weight of purified protease was estimated about 43kilodalton by SDS PAGE The optimum pH and temperature for the purified protease activity were pH 10.0 and $55^{\circ}C$, respectively. The enzyme was stable in broad range of pH 5.0 to 12.0. and at the below $45^{\circ}C$. The purified enzyme activty was inhibited by $Fe^{3+}$ and $Al^{3+}$. The activity was significantly inhibited more than 80% by O-Phenanthroline, PMSF and SDS. The $K_m$ value of the purified enzyme against Soy Protein Isolate as a substrate was 1.28 mg/ml.

• Parasites, Hosts and Diseases
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• v.31 no.4
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• pp.353-362
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• 1993

The present study was carried out to investigate the localization and isozyme patterns of acid phosphatase and alkaline phosphatase in metacercariae and in adults of F. seoulensis by enzyme-histochemistry method and electrophoresis. Acidphosphatase showed a strong activity at pH 5 in the intestinal caecum of adults, but showed no reactions in the nonsubstrate control and in the inhibitor-treated control. Alkaline phosphatase showed a strong activity at pH 8 in the intestinal caecum and the tribocytic organ of adults, and in the intestinal caecum and in the genital anlagen of metacercariae. In non-denature PAGE, ten bands of protein fraction from the extracts of metacercariae and twenty-two bands from adults were detected. In denature PAGE, two protein bands having molecular weights of 192 kDa and 123 kDa were detected in the metacercariae, but absent from adult stage. In adults, protein fractions of 27.5 kDa, 24.5 kDa, 21.4 kDa, 18 kDa, 16 kDa and 15 kDa were detected. In non-denature PAGE, isozymes of acid phosphatase showed the most strong activity at pH 5, whereas no activity was shown at pH 2 and pH 7. One isozyme 85 kDa, 73 kDa and 62 kDa) in adults.

• Journal of Life Science
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• v.7 no.3
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• pp.228-233
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• 1997

A thiol protease has been isolated and partially purified from encysted brine shrimp Artemia franciscana using a four-step procedure(filtration, salting out, gel filtration and ion exchange chromatography). The optimum pH of the enzyme for caseinolytic activity was appeared to be 3.0, and the enzymematic activity was stable up to pH 6.0 but lost completely at the pH higher than 8.0. The optimal temperature of the enzyme was appeared to be 35$^{\circ}$C, and ninety percent of the enzyme activity was lost at 45$^{\circ}$C. Various metal ions, e.g., zinc, copper, iron, inhibited the enzyme activity; however, heavy metal chelator, e.g., EDTA, stimulated the enzyme activity. The protease was concluded to be a member of the thiol group protease, since it was inhibited by thiol protease inhibitors and iodoacetate. The protease was also concluded to be a acid protease based on optimum pH.

• Applied Biological Chemistry
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• v.44 no.4
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• pp.219-223
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• 2001

Effects of hemoglobin (Hgb) concentration and degree of hydrolysis (DH) of Hgb on the separation of heme-iron were examined to produce highly enriched heme-iron from Hgb hydrolysate. Separation efficiency of Hgb hydrolysate with different DH was studied at wide pH range (pH $1.0{\sim}11.0$). Separation efficiency expressed as heme-iron/peptide ratio increased with decreasing Hgb concentration. When 5% Hgb (pH 10.0) was hydrolyzed using commercially available Esperase for 5 h at $50^{\circ}C$, DH was 25%. The precipitation of heme-iron-enriched peptides were remarkably high at pH range $3{\sim}6$. Optimal pH range for heme-iron with high heme-iron/peptide ratio shifted to acidic pH with increasing DHs of Hgb. The enriched heme-iron fraction in the precipitates showed a single band through urea-SDS-PAGE, with a molecular mass of 1 kDa. In the dry heme-iron product produced in a pilot bioreactor, content of heme-iron and heme-iron/peptide ratio were 27.1 and 38.7%, respectively, and production yield was 9.3%.

• Microbiology and Biotechnology Letters
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• v.16 no.2
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• pp.163-167
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• 1988

The conditions for the protoplast fusion of auxotrophic mutants of Penicillium verruculosum were determined. A preparation of commercial enzyme Novozym 234 was used to successfully isolate protoplast from the 20hr old mycelium of P. verruculosum. Under optimal condition, the protoplast yield ranged from 2.4$\times$10$^7$ to 3.0$\times$10$^7$ protoplasts from 400mg of damp mycelia of various auxotrophic mutant strains. The regeneration frequency ranged from 26.6 to 42.4% and the spontaneous reversion frequency of the protoplasts on the regeneration minimal medium was less than 10$^7$. The optimal concentration of PEG 6000 was 20%, and exposure of protoplasts to PEG for 10 min was found to be sufficient for protoplast fusion. Optimal pH of fusion mixture was deter-mined as 5.5 and l0mM of calcium chloride in fusion mixture effectively enhanced the protoplast fusion frequency. Under optimal condition, the fusion frequency between various auxotrophs ranged from 1.8$\times$10$^{-3}$ to 3.5$\times$0$^{-3}$.