• Journal of Microbiology and Biotechnology
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• v.31 no.6
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• pp.823-832
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• 2021

Mushroom cultivation along with the palm oil industry in Malaysia have contributed to large volumes of accumulated lignocellulosic residues that cause serious environmental pollution when these agroresidues are burned. In this study, we illustrated the utilization of lignocellulolytic enzymes from the spent mushroom substrate of Pleurotus pulmonarius for the hydrolysis of palm oil mill effluent (POME). The hydrolysate was used for the production of biohydrogen gas and enzyme assays were carried out to determine the productivities/activities of lignin peroxidase, laccase, xylanase, endoglucanase and β-glucosidase in spent mushroom substrate. Further, the enzyme cocktails were concentrated for the hydrolysis of POME. Central composite design of response surface methodology was performed to examine the effects of enzyme loading, incubation time and pH on the reducing sugar yield. Productivities of the enzymes for xylanase, laccase, endoglucanase, lignin peroxidase and β-glucosidase were 2.3, 4.1, 14.6, 214.1, and 915.4 U g^-1, respectively. A maximum of 3.75 g/lof reducing sugar was obtained under optimized conditions of 15 h incubation time with 10% enzyme loading (v/v) at a pH of 4.8, which was consistent with the predicted reducing sugar concentration (3.76 g/l). The biohydrogen cumulative volume (302.78 ml H₂.L^-1 POME) and 83.52% biohydrogen gas were recorded using batch fermentation which indicated that the enzymes of spent mushroom substrate can be utilized for hydrolysis of POME.

• Journal of Microbiology and Biotechnology
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• v.3 no.2
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• pp.86-90
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• 1993

CMCase positive clones were screened from Cellulomonas sp. YE-5 and named pCE1, pCE2 and pCE3. Among the positive clones pCE1 was used for this study, because it has the smallest insert and the highest CMCase activity among the 3 clones, and its nucleotide sequence was determined. The CMCase gene in pCE1 was composed of 1071 bp of nucleotides coding 357 amino acids. Computer analysis showed that the pCE1 has 65% sequence homology with the endoglucanase from Cellulomonas fimi.

• Journal of Animal Science and Technology
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• v.57 no.7
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• pp.23.1-23.6
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• 2015

Cellulose degrading bacteria from koala faeces were isolated using caboxymethylcellulose-Congo red agar, screened in vitro for different hydrolytic enzyme activities and phylogenetically characterized using molecular tools. Bacillus sp. and Pseudomonas sp. were the most prominent bacteria from koala faeces. The isolates demonstrated good xylanase, amylase, lipase, protease, tannase and lignin peroxidase activities apart from endoglucanase activity. Furthermore many isolates grew in the presence of phenanthrene, indicating their probable application for bioremediation. Potential isolates can be exploited further for industrial enzyme production or in bioremediation of contaminated sites.

• 한국신재생에너지학회:학술대회논문집
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• 2008.05a
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• pp.225-228
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• 2008

This study shows that lignocellulosic biomass saccharification work has been carried out with rice-straw by the extracellular enzyme from KMU001, and the enzymes produced in 5%(w/v) wood biomass were characterized by protein and various enzyme activity measurements. Several cellulases such as Endoglucanase(EG), $\beta$-D-1,4-Glucosidase(BGL), Cellobiohydrolase(CBH), and $\beta$-D-1,4-Xylanase (BXL) were detected. Saccharification of rice-straw by the enzyme yielded about 233mg/g of glucose after 48hrs.

• Korean Journal of Microbiology
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• v.24 no.3
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• pp.236-242
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• 1986

The nucleotide sequence of the genetic control site of Bacillus subtilis gene for $(1-4)-{\beta}-D-glucan$ endoglucanase (cellulase) was determined according to the procedures of the dideoxy chain termination method(Sanger et. al., 1977). The deduced amino acid sequence of this enzyme has a hydrophobic signal peptide at the $NH_2$ terminus similar to those found in fifteen other extracellualr enzymes from Bacillus species. This is followed by a sequence resembling the Bacillus ribosome binding site 14 nucleotide before the first codon of the gene. The presumptive promoter sequence was located 92 base pairs upstream fromthe initiation codon. The homology region in signal sequences was striking when comparing all the signal sequences of sixteen extracellular enzymes from Bacillus species so far compiled.

• Proceedings of the KSAR Conference
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• 2002.06a
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• pp.94-94
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• 2002

Increasing competition in the livestock industry has forced producers to cut costs by adopting new technologies aimed out increasing production efficiency. Non-ruminant livestock do not express fibrolytic enzymes. The major plant cell wall components of cereals, primarily β-glucans and arabinoxylans, form gel-like structures in the small intestines that trap nutrients. The viscous polysaccharides can also cause severe gastrointestinal disorders. (omitted)

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.202-205
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• 2000

A gene coding $endo-{\beta}$,-1, 4 glucanase from Actinomyces sp. KNG40 and phytase from Hansenula polymorpha were cloned into Esherichia coli JM101 by using E. coli/Lactobacillus shuttle vector pNZ3004 and pNZ123. The plasmid p3PS(1-4) and p123(1-4) have slpA promoter and slpA signal sequence. So, I constructed expression vectors, p3PS(1-4)Endo, phy and p123(1-4)Endo, phy. These constructed vector was transformed in target host Lactobacillus gasseri and reutri. These transformed host expressed endoglucanase and phytase as extracellular fraction. In the enzyme activity of the same vector, host L, gasseri was higher activity than L. reuteri. This indicates that L. gasseri recongnize promoter and signal sequence very well.

• Proceedings of the Korean Society of Life Science Conference
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• 2008.10a
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• pp.50.1-50.1
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• 2008

• Journal of Microbiology
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• v.43 no.6
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• pp.487-492
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• 2005

This study demonstrated that the brown rot basidiomycete Fomitopsis palustris was able to degrade crystalline cellulose (Avicel). This fungus could also produce the three major cellulases (exoglucanases, endoglucanases, and $\beta-glucosidase$) when the cells were grown on $2.0\%$ Avicel. Avicel degraded by F. palustris showed a decrease in relative crystallinity from $83\%\;to\;78.5\%$ after 14 days of incubation. The characterization study indicated that optimum pH was 4.5 and optimum temperature was $70^{\circ}C$ for exoglucanase (cellobiohydrolase) activity. Hydrolysis of Avicel by the crude enzyme from F. palustris yielded 1.6 mg/ml of glucose after 43 h, which corresponded to a cellulose conversion degree of $3.2\%$. Therefore, this study revealed for the first time that the brown rot basidiomycete F. palustris produces cellulases capable of yielding soluble sugars from crystalline cellulose.

• Plant Resources
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• v.8 no.3
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• pp.175-180
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• 2005

Thin sections of cellulose fibers were incubated with an endo- and an exoglucanase labeled with gold particles of differing sizes. The hydrolytic sites were then visualized under transmission electron microscopy (TEM). The potential interaction between the ${\beta}$-1, 4-glucan substrates and the endo- and the exoglucanases was investigated using cellulosic and lignocellulosic substrates. The simultaneous visualization was very successful in distinguishing preferred substrates for each cellulase in lignocellulosic substrates. When plant lignocellulose was preincubated with endocellulase, density of the gold labeling greatly increased suggesting that preliminary exposure of lignocellulosic material to endocellulase may have enhanced the accessibility of the substrate to endocellulase and exocellulase. This result provided a plausible explanation for the observed endo/exo cellulase co-hydrolysis.