• Korean Journal of Agricultural Science
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• v.25 no.1
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• pp.131-137
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• 1998

The cellulase components were partially purified from the culture filtrate of the alkalophilic bacterium Pseudomonas sp. AC-711 and its enzymatic properties were characterized. The specific activity of the purified major enzyme component was 3.5 units/mg protein as carboxymethyl cellulase and the yield was 23% of the total activity of the culture broth. The molecular weight of the component was 46,000 and the Km and Vmax on CMC were determined as $15.4mg\;mL^{-1}$ and $4.17{\mu}moles\;mL^{-1}\;min^{-1}$, respectively. The enzyme was stable at the temperatures below $60^{\circ}C$ and at the pH range of 4.0~11.0, and the optimal temperature and pH were $60^{\circ}C$ and pH 8.0, respectively. The enzyme activity was not significantly affected by the common surfactants (concentration: 0.05%) such as ${\alpha}$-olefin sulfonate, linear alkylbenzene sulfonate, sodium dodecyl sulfonate, hexadecyltrimethylammonium bromide and Tween 80. The enzyme was activated by the metal ions such as $Ca^{2+}$, $Cu^{2+}$, $Co^{2+}$, whereas inhibited by $Hg^{2+}$ and $Zn^{2+}$. The enzyme exhibited relatively high activity toward amorphous CMC as compared with crystalline substrates such as filter paper and avicel.

• Korean Journal of Microbiology
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• v.41 no.1
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• pp.81-86
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• 2005

One of the endoglucanases, F-I-III, was purified from the culture filtrate of T. sp. C-4 through procedures including chromatography on Sephacryl S-200, DEAE-Sepharose A-50, and Chromatofocusing on Mono-P (FPLC). The molecular weight of the enzyme was determined to be about 56,000 Da by SDS-PAGE, and pI of 4.9 by analytical isoelectric focusing. F-I-III showed the highest enzyme activity at $55^{\circ}C$, and the pH optimum of the enzyme was 5.0. There was no loss of activity when the enzyme was incubated at $50^{\circ}C$ for 24 hours. The specific activity of the enzyme F-I-III toward the CMC was 315.4 U/mg. The Km value for $PNPG_2$ of F-I-III was 2.69 mM. N-terminal sequence of F-I-III was analyzed to be QPGTSTPEVHPKKLTTYK. It showed $95\%$ of homology to that of EGI from T. reesei. The presence of some metal ions (1 mM) had only a little effect on CMCase activity. The treatment of the reducing agents resulted in the increase of endoglucanase activity.

• Microbiology and Biotechnology Letters
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• v.15 no.6
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• pp.388-395
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• 1987

In order to obtain a regulatory mutant strain with high cellulase activity, a newly isolated Penicillium verrculosum, strain F-3 was used as parental strain since it was proved to be an efficient cellulase producer. A number of experiments were conducted to determine the optimum conditions to in-duce mutagenesis and isolate the desirable mutant strains. Out of several restriction compounds tested, 1.5% oxgall was found to be most effective to restrict the colony size by suppressing overgrowth. Derepression of catabolites was employed as a criterion in selecting mutant strains with high cellulase productivity. Production of cellulase by Penicillium venculosum F-3 was suppressed when cultured on the media with more than 1% of glucose or glycerol. It was found that either irradiation with UV light for 19 mins or treatment with nitrosoguanidine at 200$\mu\textrm{g}$/m1 for 60 mins, induced mutagenesis at desired level, when the survival rate of the spore was 0.2% and 48%, respectively. Three mutant strains of F-3, UV-9, UV-10, and NTG-3 that had the highest cellulase productivity were finally selected, based on filter paper degradation rate, size of clearing zone on the screening plate and cellulase activity in the medium containing cellulose powder. When the mutant strains were compared with parental strain F-3, on the KC-M-W medium containing cellulose powder, the filter paper activities of UV-9, UV-10, and NTG-3 were increased by 34%, 55%, and 41%, respectively. However, the assimilation of cellobiose octaacetate by UV-9 or NTG-3 was markedly reduced. When the mutant UV-10 was grown on cellobiose octaacetate medium (CCA-4) in shaking flasks, the cellulase activities of the mutant increased by 20 to 50% compared to the parental strain. Excreation of soluble protein from the mutant also elevated up to 30%. The mutant also constitutively produced both CMCase and $\beta$-glucosidase, though at relatively low level, in the presence of glucose or cellobiose as carbon sources.

• Korean Journal of Food Science and Technology
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• v.3 no.3
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• pp.178-184
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• 1971

Samples of refined soybean oil were irradiated with lights from a 20-watt incandescent tungsten lamp, a 20-watt fluorescent daylight type lamp, a 20-watt low-pressure mercury vapor germicidal lamp, and direct sunlight for an experimental period of 147 days. Some samples were stored in a dark room throughout the period as a control. The peroxide values of all samples were measured every week. The induction period of the samples was arbitrarily taken as the time required for the samples to reach a peroxide value of 15. The induction period of the control was estimated at 198 days. Those of the samples irradiated with the incandescent light, the fluorescent light, the ultraviolet light, and the sunlight were estimated at 196, 119, 52 and 6 days, respectively. The sunlight showed by far the strongest prooxidant activity whereas the incandescent light showed the weakest but distinct prooxidant activity. The small temperature differences observed among the various samples throughout the experimental period did not seem to affect the oxidation rates of the irradiated samples in any significant way.

• The Korean Journal of Mycology
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• v.1 no.2
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• pp.15-23
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• 1973

Mold producing cellulase were isolated from rotten woods, and identified as the three species: Aspergillus niger van Tieghem, Aspergillus schiemanni Thom and Trichoderma viride Pers. In this paper, culture conditions in the media and characteristics of these strains were investigated. Using these strains, we have conducted a research concerning the utilization of farm product waste materia's. 1. Optimum conditions for the cellulase formation were as follows. KM 10-1; pH 5.2-5.5, $35^{\circ}C$, incubation time 6 days. OL 11-1; pH 5.5, $30-35^{\circ}C$, incubation time 6 days. SH 9-2; pH 5.5, $30^{\circ}C$, incubatoin time 6 days. 2. Their cellulase activities in their optimum condition were as follows: KM 10-1; CMC-LP 78.5% CMC-SP 4.0 glucose mg/gm of the cultures/min. OL 11-1; CMC-LP 89.9%, CMC-SP 4.9 glucose mg/gm of the cultures/min. SH 9-2; CMC-I.P 77.4%, CMC-SP 3.9 glucose mg/gm of the cultures/min. 3. Hydrolysis of animal feed containing a large quantity (23-30%) of cellulose by means of the crude enzyme in the selected strains resolved 30% of the cellulose contained in the animal feed.