• Applied Biological Chemistry
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• v.12
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• pp.99-105
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• 1969

The yield of cellulase derived from Trichoderma $(O_2-1)$ was remarkably varied with various concentration of ethanol and acetone in purification of the enzyme. In the purification with ethanol of ${\beta}-glucosidase$, the best result was obtained in the concentration of 60% and, of CMCase and of filter paper disintegrating enzyme 80%. And in the purification with acetone of ${\beta}-glucosidase$, filter paper disintegrating enzyme, and CMCase, in the concentration of 60%, 80%, and 90% respectively, was shown the best yield. The activities of crude Cellulase preparation could be seperated into few of fractions by column chromatography with Silica gel, Cellulose powder, and gauze. Most of CMCase, avicelase, and ${\beta}-glucosidase$ were eluted, but most of filter paper disintegrating enzyme and the rest of enzymes mentioned the above were absorbed, and were eluted with water. Therefore, it was considered that CMCase is different from filter paper disintegrating enzyme in properties. The relative activity of CMCase was different from that of avicelase in the peak of elusion part. And it was considered that filter paper disintegrating enzyme and cellulose powder saccharifying enzyme was seperated respectively as absorption part and non absorption part. The auther came to the conclusion that at least there were more than three sorts of cellulase in Trichoderma $(O_2-1)$ cellulase preparation.

• Journal of Life Science
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• v.18 no.3
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• pp.323-328
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• 2008

In this study we evaluated the method to develop red ginseng oil containing high content of phytochemicals by enzymes treatment. To select the optimum extraction process of red ginseng with oils, the antioxidant activities of red ginseng using various enzymes were measured. Red ginseng after 0.5% cellulase treatment for 1 hr at $50^{\circ}C$ had higher antioxidant activity than the other conditions. We found that red ginseng/soybean oil extracted for 15 days at $40^{\circ}C$ after 0.5% cellulase treatment increased DPPH radical scavenger activity and decreased the TBA and POV values. However, red ginseng/olive oil had little functional activities compare to the red ginseng/soybean 0il. We also analyzed vitamin A and E by HPLC and found that vitamin E was increased by 0.5% cellulase treatment in the oil. This is the first report that red ginseng oil extracted by enzyme treatment has various beneficial effects.

• Food Science and Preservation
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• v.24 no.1
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• pp.60-67
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• 2017

In this study, we tried to establish the best method for fresh blueberry beverage production using enzyme treatment as well as low temperature extraction. During extraction of physiologically functional materials, we used low temperature to prevent nutritional loss by heat. In addition, we investigated optimal blueberry extraction conditions using various enzyme treatments (cellulase, pectinase, cellulase:pectinase (1:1) mixture) to increase extraction efficiency and reduce turbidity. A variety and ratio of enzymes, extraction temperature, extraction time, and shaking speed were considered for the best extraction efficiency rate. We observed high extraction efficiency rates of 85.72-86.55% and 87.06-87.93%, respectively, upon cellulase or pectinase treatment. In addition, a mixture of cellulase:pectinase (1:1) showed an extraction efficiency rate of 86.84-88.14%. The best extraction efficiency rate was observed when crude blueberry was treated at $45^{\circ}C$ (87.91%), for 3 h (87.88%), in a 90 rpm shaker (89.19%). Sugar content and acidity of blueberry extract were not affected by the various treatments. However, total phenolic compounds were detected upon pectinase treatment (18.62 mg/g). Only fructose and glucose as free sugars were found in all samples regardless of treatments and extraction conditions.

• Asian-Australasian Journal of Animal Sciences
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• v.26 no.8
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• pp.1144-1151
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• 2013

In this study, protein domains with cellulase activity in goat rumen microbes were investigated using metagenomic and bioinformatic analyses. After the complete genome of goat rumen microbes was obtained using a shotgun sequencing method, 217,892,109 pair reads were filtered, including only those with 70% identity, 100-bp matches, and thresholds below $E^{-10}$ using METAIDBA. These filtered contigs were assembled and annotated using blastN against the NCBI nucleotide database. As a result, a microbial community structure with 1431 species was analyzed, among which Prevotella ruminicola 23 bacteria and Butyrivibrio proteoclasticus B316 were the dominant groups. In parallel, 201 sequences related with cellulase activities (EC.3.2.1.4) were obtained through blast searches using the enzyme.dat file provided by the NCBI database. After translating the nucleotide sequence into a protein sequence using Interproscan, 28 protein domains with cellulase activity were identified using the HMMER package with threshold E values below $10^{-5}$. Cellulase activity protein domain profiling showed that the major protein domains such as lipase GDSL, cellulase, and Glyco hydro 10 were present in bacterial species with strong cellulase activities. Furthermore, correlation plots clearly displayed the strong positive correlation between some protein domain groups, which was indicative of microbial adaption in the goat rumen based on feeding habits. This is the first metagenomic analysis of cellulase activity protein domains using bioinformatics from the goat rumen.

• Korean Journal of Microbiology
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• v.40 no.2
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• pp.139-146
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• 2004

A bacterium producing alkaline cellulase was isolated from soil, leaf mold and compost, and was identified as alkalophilic Bacillus sp. HSH-810 by morphological, cultural and biochemical determination. The optimum cul-ture condition of Bacillus sp. HSH-810 for the growth and alkaline cellulase production was $30^{\circ}C$ and pH 10.0. The maximum alkaline cellulase production was obtained when 1.0%(w/v) CMC, 0.5%(w/v) peptone, 0.02%(w/v) $CaCl_2$ and 0.02(w/v) $CoCl_2$ were used as carbon source, nitrogen source and mineral source, respectively. The optimum pH and temperature of the enzyme activity were pH 10.5 and $50^{\circ}C$, respectively. This enzyme was fairly stable in the pH range of 6.0-13.0 and at $50^{\circ}C$. For the effect of surfactants, the activity of alkaline cellulase was stable in the presence of sodium-$\alpha$-olefin sulfonate (AOS), sodium dodecyl sulfonate (SDS), Tween 20 and Tween 80, but inhibited by the presence of 0.1 linear alkyl-benzene sulfonate (LAS) sig-nificantly.

• Journal of Microbiology and Biotechnology
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• v.21 no.12
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• pp.1312-1321
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• 2011

Enzyme extracts of cellulase [filter paper cellulase (FPase) and carboxymethyl cellulase (CMCase)], chitinase, and chitosanase produced by Aspergillus niger NRRL-567 were evaluated. The interactive effects of initial moisture and different inducers for FP cellulase and CMCase production were optimized using response surface methodology. Higher enzyme activities [FPase $79.24{\pm}4.22$ IU/gram fermented substrate (gfs) and CMCase $124.04{\pm}7.78$ IU/gfs] were achieved after 48 h fermentation in solid-state medium containing apple pomace supplemented with rice husk [1% (w/w)] under optimized conditions [pH 4.5, moisture 55% (v/w), and inducers veratryl alcohol (2 mM/kg), copper sulfate (1.5 mM/kg), and lactose 2% (w/w)] (p<0.05). Koji fermentation in trays was carried out and higher enzyme activities (FPase $96.67{\pm}4.18$ IU/gfs and CMCase $146.50{\pm}11.92$ IU/gfs) were achieved. The nonspecific chitinase and chitosanase activities of cellulase enzyme extract were analyzed using chitin and chitosan substrates with different physicochemical characteristics, such as degree of deacetylation, molecular weight, and viscosity. Higher chitinase and chitosanase activities of $70.28{\pm}3.34$ IU/gfs and $60.18{\pm}3.82$ to $64.20{\pm}4.12$ IU/gfs, respectively, were achieved. Moreover, the enzyme was stable and retained 92-94% activity even after one month. Cellulase enzyme extract obtained from A. niger with chitinolytic and chitosanolytic activities could be potentially used for making low-molecular-weight chitin and chitosan oligomers, having promising applications in biomedicine, pharmaceuticals, food, and agricultural industries, and in biocontrol formulations.

• The Korean Journal of Mycology
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• v.26 no.2 s.85
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• pp.239-245
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• 1998

The feasibility of enzymatic hydrolysis of cellulosic materials is dependent on the cost of cellulase, which is strongly influenced by the selection of proper carbon source in the cellulase production medium. When solka floc was used as a carbon source for the production of cellulase by Trichoderma reesei Rut C-30, a maximum of 53.2 U/ml of CMCase activity (4.8 U/ml of FPase activity) was obtained with a concentration of 1 % of solka floc. The cellulase activity decreased to 50% in the presence of 0.5% of glucose in the medium. The production of cellulase was considerably enhanced when solka floc and wheat bran were used together as a carbon source. A medium which contained 1 % of solka floc and 3 % of wheat bran yielded highest cellulase activity: CMCase activity of 76 U/ml and FPase activity of 12.5 U/ml.

• Journal of Microbiology and Biotechnology
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• v.10 no.6
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• pp.770-775
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• 2000

Several process parameters were studied to ascertain the effect on degradation of sugar cane bagasse in relation to the production of cellulase enzyme and reducing sugars by Solid Substrate Fermentation (SSF) and Submerged Culture Fermentation (SCF) of Aspergillus terreus SUK-1. The effect of air-flow rate (0-1.3 v/v/m), of different ratios of substrate weight to liquid volume (1:6, 1:10, 1:20, and 1:30 w/v, g/ml), scale-up effect (10, 20, and 100 times of 1:10 ration, w/v) and the effect of temperature (30, 40, 50, and $60^{\circ}C$) in SSF were studied. Air-flow rate of 1.0 v/v/m gave the highest enzyme activity (FPase 0.25 IU/ml, CMCase 1.24 IU/ml) and reducing sugars concentration (0.72 mg/ml). Experiment using 1:10 ratio (w/v) was found to support maximum cellulase activity (FPase 0.58 IU/ml, CMCase 1.97 IU/ml) and reducing sugar concentration (1.23 mg/ml). Scaling-up the ratio of 1:10(w/v) by a factor of 20 gave the highest cellulase activity (FPase 0.71 IU/ml, CMCase 2.25 IU/ml) and reducing sugar concentration (3.67 mg/ml). The optimum temperature for cellulase activity and reducing sugar production was $50^{\circ}C$(FPase 0.792 IU/ml, CMCase 2.25 IU/ml and 3.85 mg/ml for reducing sugar concentration). For SCF, the activity of cellulase enzyme and reducing sugar concentration was found to be lower than that obtained for SSF. The highest cellulase activity obtained in SCF was 50% lower than the highest cellulase activity in SSF, while for reducing sugar concentration, the highest concentration obtained in SCF was 90% lower than that obtained in SSF.

• Applied Biological Chemistry
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• v.11
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• pp.109-117
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• 1969

Out of some 400 strains of Microorganisms, cellulase forming organisms was isolated from night soil during the course of screening tests. Two strains, Ku-3371 and Ku-4383 were found capable of producing cellulase in the shaking culture. General properties of the crude enzyme were as the following results. 1. The optimum pH values on CMC-saccharifying, CMC-liquefying and filter paper disintegrating activities were 4.0 to 5.5. 2. The stable pH range was within 3.5 to 6.5, 3. The optimum temperature was $40-45^{\circ}C$, the thermal stability was below $50^{\circ}C$ except on paper disintegrating activity and completely inactivated at $70^{\circ}C$. 4. Dialyzed crude enzyme was activated by $Mn^{2+}\;and\;Co^{2+}$ repectively but $Hg^{2+}$ was strong inhibitor.

• Korean Journal of Soil Science and Fertilizer
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• v.44 no.5
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• pp.836-840
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• 2011

In order to isolate thermophilic compost-promoting bacteria with high activity of cellulase and xylanase, spent mushroom substrates with sawdust were collected from mushroom cultivation farm, Jinju, Gyeongnam in Korea. Among of the isolates, one strain, designated SJ21 was selected by agar diffusion method. The strain SJ21 was identified as members of the Bacillus lincheniformis by biochemical characteristics using Bacillus ID kit and VITEK 2 system. Comparative 16S rDNA gene sequence analysis showed that strain SJ21 formed a distinct phylogenetic tree within the genus Bacillus and was most closely related to Bacillus subtilis with 16S rDNA gene sequence similarity of 99%. On the basis of its physiological properties, biochemical characteristics and phylogenetic distinctiveness, strain SJ21 was classified within the genus Bacillus, for which the name Bacillus sp. SJ21 is proposed. The cellulase and xylanase activity of Bacillus sp. SJ21 was slightly increased according to bacterial population from exponential phase to stationary phase in growth curve for Bacillus sp. SJ21.