• The Korean Journal of Food And Nutrition
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• v.11 no.3
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• pp.319-322
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• 1998

The whole cell of alkalophilic Streptomyces sp. B-2 which produce glucose isomerase was immobilized by entrapment method for the effective production of high fructose syrup. The highest immobilized activity was achieved when the enzyme was bound to 2% $textsc{k}$-carrageenan. Immobilized glucose isomerase the pH optimum was about pH 7.5~8.5. Immobilization of alkalophilic Streptomyces sp. B-2 on 2% $textsc{k}$-carrageenan at 7$0^{\circ}C$ showed an increase in glucose isomerase activity. GI activity of immobilized cells was maximum Co2+ concentration 10-3M, Mg2+ concentration 10-3M.

• KSBB Journal
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• v.21 no.5
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• pp.384-388
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• 2006

The production stability of high-yielding mutants of Streptomyces lincolnensis immobilized on celite beads was examined in repeated batch cultures. We also explored the feasibility of immobilization of vegetative mycelial cells on pre-wetted celite beads, which is practical method for cell immobilization. Repeated transfer of immobilized cells into fresh medium every 10 days increased productivity of immobilized cells and maximum concentration of lincomycin, 1007 $({\pm}256)$ mg/L, was obtained at the end of the ninth cycle. A 1.4-fold higher productivity was obtained in immobilized-cell culture than that obtained by suspended-cell culture. When pre-wetted beads were inoculated with vegetative mycelia and cultured a slightly higher amount of immobilized cells and lincomycin was obtained more than those obtained by culture of spores immobilized on dry beads. This result indicates that immobilization of mycelial cells on pre-wetted beads was readily available. This technique is simple and no additional facilities are required for cell immobilization.

• Journal of Microbiology and Biotechnology
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• v.12 no.4
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• pp.557-562
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• 2002

Physiological characteristics such as specific productivity, morphology of Streptomyces cells Immobilized on celite beads, and operational stability at different dilution rates were investigated in continuous immobilized-cell cultures for the production of kasugamycin. At a dilution rate (D) of 0.05 $h^{-1}$, a relatively high specific productivity was attained and the loss of cell-loaded beads was negligible. At D=0.1 $h^{-1}$, a higher specific productivity and cell concentration could be obtained, resulting in a significantly improved volumetric kasugamycin productivity. However, no stable operation could be maintained due to a significant loss of cell-loaded beads from the reactor that was caused by their fluffy morphology developed in the later stage. At D=0.2 $h^{-1}$, the production of kasugamycin and cell growth were observed to be severely inhibited by the high concentration of residual maltose.

• Journal of Microbiology and Biotechnology
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• v.2 no.2
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• pp.78-84
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• 1992

Streptomyces sp. No.8, which produced glucose isomerase was isolated from soil samples. The isolated strain, No.8, was identified as belonging to the Genus Streptomyces. A mutant strain, SM 805, showed the greatest ability to produce glucose isomerase. It was developed from the strain, No.8, by mutagenesis induced by NTG and UV treatment. The mutant strain, SM 805, produced about 7 times more glucose isomerase than the parental strain, No.8. This enzyme catalyzed the isomerization of D-xylose, D-glucose and D-ribose. It was inactive in the absence of metal ions, but was activated by the addition of $Mg^{2+}$ or $Co^{2+}$. The optimum temperature and pH for enzyme activity were $80^\circ{C}$ and pH 8.5, respectively. The enzyme was stable in a pH range of 6.0 to 10.0, and it was highly thermostable. There was no activity loss below $80^\circ{C}$, and even above $90^\circ{C}$ about 45% of its activity was retained. The reaction equilibrium was reached when about 53% fructose was present in the reaction mixture. Whole cells containing glucose isomerase from Streptomyces sp. SM 805 were immobilized by glutaraldehyde treatment. The resultant immobilized enzyme pellets showed a relatively long stability during the isomerizing reaction. The half-life of the immobilized enzyme during the operating was 45 days in the presence of 10mM $Mg^{2+}$.

• Journal of Microbiology and Biotechnology
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• v.22 no.9
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• pp.1218-1223
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• 2012

${\varepsilon}$-Poly-$_L$-lysine (${\varepsilon}$-PL), produced by Streptomyces or Kitasatospora strains, is a homo-poly-amino acid of $_L$-lysine, which is used as a safe food preservative. The present study investigates the combined use of cell immobilization and in situ adsorption (ISA) to produce ${\varepsilon}$-PL in shaken flasks. Loofah sponge-immobilized Streptomyces ahygroscopicus GIM8 produced slightly more ${\varepsilon}$-PL than those immobilized on synthetic sponge, and sugarcane bagasse. Moreover, loofah sponge supported the maximum biomass. Hence, loofah sponge was chosen for cell immobilization. Meanwhile, the ion-exchange resin D152 was employed for ISA. The loofah sponge-immobilized cells produced $0.54{\pm}0.1g/l$ ${\varepsilon}$-PL, which significantly increased to $3.64{\pm}0.32g/l$ after combining with ISA through the addition of resin bags. The free cells with ISA using the dispersed resin yielded $2.73{\pm}0.26g/l$ of ${\varepsilon}$-PL, an increase from $0.82{\pm}0.08g/l$. These data illustrate that the proposed combination method improved production most significantly compared with either immobilization or ISA only. Moreover, the immobilized cells could be repeatedly used and an ${\varepsilon}$-PL total amount of $8.05{\pm}0.84g/l$ was obtained. The proposed combination method offers promising perspectives for ${\varepsilon}$-PL production.

• Microbiology and Biotechnology Letters
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• v.19 no.4
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• pp.405-412
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• 1991

The enzymes were immobilized by treating the microbial cells in 0.05% chitosan and 0.28% glutaraldehyde solution. The activity of immobilized cell was about 535 IGIC/g. Glucose isomerase was purified by 6.5 times after homogenization using 60% $(NH_4)_2S0_4$ fractionation, DEAE-cellulose and Sephadex G-150 gel filtration. The molecular weight of enzyme was about 140,000 when it was measured by HPLC and the purified enzyme had only one band by electrophoresis. It showed good enzyme activity at pH 7.5 and $75^{\circ}C$. The optimum conditions for enzyme reactions were shifted to pH 7.0 and $80^{\circ}C$ when the enzyme was immobilized. The enzyme reaction was activated by the addition of 5~10 mM magnesium ion and the thermostability was improved by the addition of 0.25 mM cobalt ion. The enzyme activity was competitively inhibited by sugar alcohols.

• Clean Technology
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• v.4 no.1
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• pp.45-59
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• 1998

Continuous immobilized-cell culture was carried out for the production of kasugamycin, a secondary metabolite by a filamentous bacteria, Streptomyces kasugaensis, with an intention of reducing waste generation. A sporulation medium was developed for production of bulk amounts of spores, and the spores were entrapped into celite biosupports for immobilization. It was possible to effectively keep the immobilized-cells inside the reactor during the continuous culture by an efficient immobilized cell separator of decantor type on the outlet of the fermentor. Using this continuous immobilized-cell fermentor system, we investigated the effects of feed substrate and phosphate concentrations on kasugamycin production and chemical oxygen demand(COD). Comparing with the conventional suspended-cell batch culture, the kasugamycin productivity was observed to increase by 2.5 times, whereas COD per unit kasugamycin production decreased by 2.3 times in the continuous immobilized-cell culture. Based on these results, the continuous immobilized-cell system was considered to be a cleaner bioprocess than the conventional batch suspended-cell system.

• Korean Journal of Food Science and Technology
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• v.11 no.3
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• pp.192-199
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• 1979

With cells of Streptomyces spp K-45 isolated from soil, the immobilization of glucose isomerase by a series of treatments ; heat, carefully manipulated drying, extrusion with a thickening agent, and glutaraldehyde-induced crosslinking, was presented. This was aimed to obtain a mechanically stable form of whole cell containing glucose isomerase. The resulted pellet form had a good mechanical strength, compared with a commercial product, and showed 26 % of the activity recovery. The specific activity was 48.1 units per g of the dry material. The immobilized glucose isomerase generally showed properties similar to those of the soluble enzyme ; optimal pH at $7.5{\sim}9.0$, optimal temperature at $80{\sim}85^{\circ}C$, activation energy of 10.9 kcal/mole, and $K_m$ for glucose of 10.9M. The immobilized enzyme was very thermostable and pH stable.