• Asian-Australasian Journal of Animal Sciences
• /
• v.12 no.4
• /
• pp.531-536
• /
• 1999

This study was conducted to compare the effects of lactic acid bacteria (LAB) or LAB+cellulases on the cell wall compositions and the in vitro dry matter digestibility (IVDMD) of Rhodesgrass (RG) and Italian ryegrass (IRG) silages. LAB (Lactobacillus cassei) at a concentration of $10{\times}10^5\;cfu.g^{-1}$ fresh forage was added to all ensiling samples (except the untreated control) of RG and IRG. The cellulases used were Acremoniumcellulase (A), Meicelase (M) or a mixture of both (AM). Each cellulase was applied at levels of 0.005, 0.01 and 0.02 % fresh sample. The samples were incubated at 20, 30 and $40^{\circ}C$ for about 2 months of storage. LAB inoculation did not affect cell wall components or IVDMD of both the RG and IRG silages, but LAB+cellulase treatments did. Increasing the amount of cellulase addition resulted in further decreases of cell wall concentrations. This reduction more markedly occurred with cellulases A and AM than it did with cellulase M. Cell wall components losses were higher in the IRG silages than in the RG silages. LAB+cellulase treatments decreased IVDMD of the RG silages, but had no effect on the IRG silages. The different effect of LAB+cellulase treatments on cell wall degradation and IVDMD of the RG and IRG silages suggested that RG contains more structural carbohydrates, which were difficult to degrade with cellulase, than did IRG.

• Microbiology and Biotechnology Letters
• /
• v.30 no.1
• /
• pp.98-102
• /
• 2002

Lignocellulosic wastes available in abundance can be excellent substrates for the production of cellulase. Different types of substrates and various pretreatments were used to improve the production of cellulase. The steam-exploded wood chip gave the highest activities of FPase (0.84 IU/mL) and CMCase (6.5 IU/mL) in the shake-flask culture. In 30 L bioreactor the steam-exploded wood chip and residue after saccharification gave the FPase activity (0.72 IU/mL) and the CMCase activity (6.3 IU/mL), respectively, similar those obtained in lactose.

• Journal of Korea Technical Association of The Pulp and Paper Industry
• /
• v.30 no.1
• /
• pp.18-28
• /
• 1998

The main protein peak was observed in fraction No.9 and 109 when cellulase seperation was conducted by use of DEAE-Sephadex. The protein obtained from fraction No.9 has the characteristics of Cx component and that from fraction No.109 characteristics similiar to $C_1$ component. The effective reaction condition of the ensyme used was $40^{\circ}C$ in temperature. pH 5.0 and 90 minutes in treatment time. For the case of $C_1$ pH 5.5 in temperature range of $30^{\circ}C 50^^{\circ}C$, 4.0 5.5 in pH, and over 30 minutes of treatment time, the reaction was in the range of 80% of the maximum. Affinity of enzyme increased as freeness, increased, and this effect was more visible in fiber than in fines.

• Journal of the Korean Graphic Arts Communication Society
• /
• v.16 no.3
• /
• pp.157-170
• /
• 1998

To investigate the most effective way of cellulase utilization on paper making process and the systematic way of how to combine its components for better use, purified two major cellulase were applied to bleached kraft pulp at various dosage in the refining process and estimated the synergism effect of each components in the characteristics of papermaking fiber. freeness was not changed by $C_1$ Component dosage but strongly increased by Cx Component dosage. Drop in fiber viscosity, increase in WQV, fiber shortening and fine generation was strongly influenced by Cx Component, it seems to be that Cx Component works a hydrogenate that breaks hydrogen bonding in fiber and enhances pooling effect of fiber. $C_1$ Component was little influenced these characteristics of fiber but considered to help to make fiber surface smooth.

• Journal of Radiation Industry
• /
• v.11 no.3
• /
• pp.145-149
• /
• 2017

The cel7A sequence variation was analyzed between the wild type (Lentinula edodes KACC42378) and its cellulase activity enhanced mutant LER277. LER277 was induced by using gamma ray radiation ($^{60}Co$) at the $LD_{99}$ dose (0.94 kGy). Cloning and sequencing results showed that the cel7A coding DNA sequence (CDS) of LER277 had five nucleotide substitutions ($T{\rightarrow}C$, 201, 285 and 744 nt; $A{\rightarrow}G$, 525 nt; $C{\rightarrow}T$, 540 nt) and one hexanucleotide repeat insertion (GGCACC, within 1375-1392 nt) compared to that of the wild type. The Five nucleotide substitutions did not change the deduced amino acids and the hexanucleotide insertion elongated the GT repeat in a serine/threonine/glycine-rich linker. These results suggest that the enhancement of the cellulase activity in LER277 partly stemmed from cel7A changes by which the GT repeat of the linker is elongated.

• Korean Journal of Microbiology
• /
• v.25 no.4
• /
• pp.293-303
• /
• 1987

A $C_{1}$ enriched cellulase fraction was separated from culture filtrate of anaerobic Clostridium thermocellum by hydroxyapatite column chromatography. The separated fraction showed strong synergistic action with $C_{x}$ component (endo-$\beta$-1, 4-glucanase) in digestion of crystalline cellulose, similar to the other aerobic cellulolytic microorganisms. Unlike the $C_{x}$ component the $C_{1}$ enriched fraction was rapidly inactivated by oxidation at the atmospheric condition. The enzyme activity was significantly enhanced by the addition of reducing agents, especially $\beta$-mercaptoethanol, which indicates that a $C_{1}$ component has a lot of sulfhydryl groups essential for the enzyme activity. The effect of metal ions on $C_{1}$ activity was also investigated. The $C_{1}$ fraction was found to be thermally stable compare to endo-$\beta$-1,4-glucanase. Optimal temperature and pH were found to be $60^{\circ}C$ and 6.0, respectively.

• Korean Journal of Microbiology
• /
• v.35 no.4
• /
• pp.277-282
• /
• 1999

A bacterium producing the extracellular cellulase was isolated from cattle feces and screened as cellulase activity was excellent upon congo red straining method and activity measurements. Isolate was identified as Bacillus subtilis CH-10 on the basis of morphological and biochemical properties as well as cellular fatty acids composition. The enzyme which the isolate secretes had the optimum initial pH and temperature for its induction was 7.5 and 50${\circ}C$, respectively. The maximum CMCase activity in crude enzyme solution was observed at pH 7.5 and 75${\circ}C$ and was stable for pH 7.5 to 9.0 to maintain 70% activity. When the isolate was cultured in CMC media at 37${\circ}C$ for 24 hrs, CMCase and FPase activity was 1.13 U/㎖and 0.16U/㎖, respectively whereas Avicelase and ${\beta}$-glucosidase activity was not detected. When crude supernatant was used for zymogram, three major bands, cel 1, cel 2 and cel 3, were detected approximately 39, 41 and 57 KDa, respectively on CMC-SDS-PAGE.

• Applied Biological Chemistry
• /
• v.11
• /
• pp.83-88
• /
• 1969

94 Cellulase producing strains were isoated from soils, composts, rotten woods and straws, and gastric contents and feces of herbivorous animals in various places. Among them, the strain MC-9, MC-10, MC-53 and MC-61 were found to be highly active in the degradation of carboxy methyl cellulose. Their cultural conditions adequate for the cellulase formation and effects of inorganic salts and various organic substances added to the wheat bran media were investigated. The results obtained are as follows; 1. Optimum conditions for the cellulase formation were MC-9: pH 5.5, temp. $35^{\circ}C$, incubation time 5 days, MC-10: pH 5.5-6.0, temp. $30^{\circ}C$, incubation time 5 days, MC-53: pH 3.5, temp. $30^{\circ}C$, incubation time 5 days, MC-61: pH 3.5-4.0, temp. 30-$35^{\circ}C$, incubation time 5 days. 2. Their cellulase activity in their optimum conditions were MC-9: CMC-LP(liquefying power). 87.7%, CMC-SP(saccharifying power) 3.20 glucose mg./gm. of the cultures/min., MC-10: CMC-LP 82.9%, CMC-SP 2.48 glucose mg./gm. of the cultures/min., MC-53: CMC-LP 72.4%, CMC-SP 1.76 glucose mg./gm. of the cultures/min., MC-61: CMC-LP 87.1%, CMC-SP 2.08 glucose mg./gm. of the cultures/min. 3. Additions of inorganic salts to the wheat bran media were not significant for the cellulase formation, but additions of soybean film and orange-peel pomace promoted the CMC-liquefying power 3 to 5 percent in wheat bran cultures of the strains.

• Asian-Australasian Journal of Animal Sciences
• /
• v.11 no.5
• /
• pp.522-529
• /
• 1998

This experiment was conducted to study the effects of lactic acid bacteria (LAB) inoculation either alone or in combination with cell wall degrading enzymes on the fermentation characteristics and chemical compositions of Rhodesgrass silage. Over to 1 kg of fresh Rhodesgrass sample a treatment of inoculant LAB with or without addition of an enzyme of Acremoniumcellulase (A) or Meicelase (M) or a mixture of both enzymes (AM) was applied. The treatments were control untreated, LAB-treated (application rate $1.0{\times}10^5cfu/g$ fresh sample), LAB+A 0.005%, LAB+A 0.01%, LAB+A 0.02%, LAB+M 0.005%, LAB+M 0.01%, LAB+M 0.02 %, LAB+AM 0.005%, LAB+AM 0.01%, and LAB+AM 0.02%. The sample was ensiled into 2-L vinyl bottle silo, with 9 silages of each treatment were made. Three silages of each treatment were incubated at 20, 30 and $40^{\circ}C$ for 2-months of storage period. All silages were well preserved with their fermentation quality has low pH values (3.91-4.26) and high lactic acid concentrations (4.11-9.89 %DM). No differences were found in fermentation quality and chemical composition of the control untreated silage as compared to the LAB-treated silage. Combined treatment of LAB+cellulases improved the fermentation quality of silages measured in terms of lower (p < 0.01) pH values and higher (p < 0.05) lactic concentrations than those of LAB-treated silages. Increasing amount of cellulase addition resulted in decrease (p < 0.05) of pH value and increase (p < 0.05) of lactic acid concentration. LAB + cellulase treatments (all cellulase types) reduced (p < 0.01) NDF, ADF and in vitro dry matter digestibility of silages compared with the control untreated silages. The fermentation quality and the rate of cell wall reduction were higher (p < 0.01) in the silages treated with LAB + cellulase A than in the silages treated with either LAB+cellulase M or LAB + cellulase AM. Incubation temperature of $40^{\circ}C$ was likely to be more appropriate environment for stimulating the fermentation of Rhodesgrass silages than those of 20 and $30^{\circ}C$.

• Journal of Ginseng Research
• /
• v.40 no.2
• /
• pp.121-126
• /
• 2016

Background: Ginsenoside F1, a pharmaceutical component of ginseng, is known to have antiaging, antioxidant, anticancer, and keratinocyte protective effects. However, the usage of ginsenoside F1 is restricted owing to the small amount found in Korean ginseng. Methods: To enhance the production of ginsenoside F1 as a 10 g unit with high specificity, yield, and purity, an enzymatic bioconversion method was developed to adopt the commercial enzyme Cellulase KN from Aspergillus niger with food grade, which has ginsenoside-transforming ability. The proposed optimum reaction conditions of Cellulase KN were pH 5.0 and $50^{\circ}C$. Results: Cellulase KN could effectively transform the ginsenosides Re and Rg1 into F1. A scaled-up biotransformation reaction was performed in a 10 L jar fermenter at pH 5.0 and $50^{\circ}C$ for 48 h with protopanaxatriol-type ginsenoside mixture (at a concentration of 10 mg/mL) from ginseng roots. Finally, 13.0 g of F1 was produced from 50 g of protopanaxatriol-type ginsenoside mixture with $91.5{\pm}1.1%$ chromatographic purity. Conclusion: The results suggest that this enzymatic method could be exploited usefully for the preparation of ginsenoside F1 to be used in cosmetic, functional food, and pharmaceutical industries.