• Journal of the Korean Society of Food Culture
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• v.11 no.5
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• pp.683-687
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• 1996

Jujube paste was prepared by autoclaving the fresh jujube at 1.2 atm and $120^{\circ}C$ for 30 min and removing the skin and cores. In order to increase the juice yield, the paste was treated with pectinase, cellulase and their combinations. The soluble fractions of enzymatically treated jujube paste were characterized in terms of yield, pH, titratable acidity, color, Bx, transmittance and sugar compositions. The original paste exhibited the water soluble fraction of 57.3%. Of various quality factors, the clarity was the most significantly distinguished between pectinase and cellulase treatments. The cellulase treatment produced the cloudy juice with the yield of 83.60%. On the other hand, the clear juice was produced by the pectinase and combined treatments due to degradation of pectins, whose yields were 79.47% and 85.39%, respectively. The results clearly demonstrated that the pectinase treatments improved the solubilization efficiency and clarity.

• Journal of Radiation Industry
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• v.5 no.2
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• pp.107-112
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• 2011

Electron beam-induced crosslinking of polycaprolactone (PCL) films containing various crosslinking agents (CAs) was investigated in this study. PCL films containing various CAs prepared by a solution casting method were irradiated by electron beams at various absorption doses and the irradiated PCL films were investigated in terms of their crosslinking degree, thermal and mechanical properties, and biodegradability. Based on the results of the crosslinking degree measurement, triallyl isocyanurate was found to be most effective for the electron-beam induced crosslinking of PCL films. The results of the UTM, DMA, and TMA revealed that the thermal and mechanical properties of the crosslinked PCL films were greatly improved in comparison to those of the pure PCL. The results of the enzymatic degradation test revealed that the biodegradability of the crosslinked PCL films was reduced in comparison to that of the pure PCL.

• Journal of Microbiology and Biotechnology
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• v.31 no.5
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• pp.740-746
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• 2021

Efficient cellulolytic enzyme production is important for the development of lignocellulose-degrading enzyme mixtures. However, purification of cellulases from their native hosts is time- and labor-consuming. In this study, a constitutive expression system was developed in Penicillium oxalicum for the secreted production of proteins. Using a constitutive polyubiquitin gene promoter and cultivating with glucose as the sole carbon source, nine cellulolytic enzymes of different origins with relatively high purity were produced within 48 h. When supplemented to a commercial cellulase preparation, cellobiohydrolase I from P. funiculosum and cellobiohydrolase II from Talaromyces verruculosus showed remarkable enhancing effects on the hydrolysis of steam-exploded corn stover. Additionally, a synergistic effect was observed for these two cellobiohydrolases during the hydrolysis. Taken together, the constitutive expression system provides a convenient tool for the production of cellulolytic enzymes, which is expected to be useful in the development of highly efficient lignocellulose-degrading enzyme mixtures.

• Journal of Physiology & Pathology in Korean Medicine
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• v.36 no.2
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• pp.79-87
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• 2022

In this study, extracts of Boswellia serrata gum resin, Curcuma longa rhizome, and Terminalia chebula fruit were combined in different ratios, and their anti-osteoarthritis effects were compared to determine which combination had the best synergistic effect. B. serrata, C. longa, and T. chebula extracts in a 2:1:2 ratio exhibited higher antioxidative activity in scavenging DPPH radicals than did the individual extracts alone or the other extract combinations. Additionally, the 2:1:2 combination significantly improved the levels of enzymatic antioxidants and antioxidant-related proteins. Moreover, this same combination ratio decreased the protein levels of matrix metalloproteinase (MMP) 3 and MMP13 in interleukin-1β-stimulated human articular chondrocytes (HCHs) and increased those of aggrecan and collagen type II alpha 1 chain (COL2A1). Analysis of the underlying mechanisms revealed that the 2:1:2 combination significantly inhibited the phosphorylation of nuclear factor kappa B (NF-κB) p65, extracellular regulated protein kinase (ERK), and p38 mitogen-activated protein kinase (MAPK). Therefore, the 2:1:2 combination of these three plant extracts has the best potential for use as an effective dietary supplement for improving joint health compared with the individual extracts and their other combination ratios.

• Clean Technology
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• v.28 no.1
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• pp.32-37
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• 2022

Food waste is produced from food factories, food services, and home kitchens. The generated mass reached 5.4 million tons/year in 2020. The basic management technology for such waste has been biological degradation under an anaerobic environment. However, the whole process is intrinsically slow and considerably affected by the inner physicochemical properties of the waste and other surrounding conditions, which makes optimization of the process difficult. The most promising options to counter this massive generation of waste are eco-friendly treatments or recycling. As a preliminary step for these options, attempts were made to evaluate the feasibility and usability of three simulative models based on reaction kinetics. Model (A) predicted relative changes over reaction time for reactant, intermediate, and product. Overall, an increased reaction rate produced less intermediate and more product, thereby leading to a shorter total reaction time. Particle diminishing model (B) predicted reduction of the total waste mass. The smaller particles diminished faster along with the dominant effect of microbial reaction. In Model (C), long-chain cellulose was predicted to transform into reducing sugar. At a standard condition, 48% of cellulose molecules having 10⁵ repeating units turned into reducing sugar after 100 h. Also it was found that the optimal enzyme concentration where the highest amount of remnant sugar was harvested was 1 mg L^-1.

• BMB Reports
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• v.57 no.7
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• pp.318-323
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• 2024

Regulation of cell fate and lung cell differentiation is associated with Aminoacyl-tRNA synthetases (ARS)-interacting multifunctional protein 2 (AIMP2), which acts as a non-enzymatic component required for the multi-tRNA synthetase complex. In response to DNA damage, a component of AIMP2 separates from the multi-tRNA synthetase complex, binds to p53, and prevents its degradation by MDM2, inducing apoptosis. Additionally, AIMP2 reduces proliferation in TGF-β and Wnt pathways, while enhancing apoptotic signaling induced by tumor necrosis factor-α. Given the crucial role of these pathways in tumorigenesis, AIMP2 is expected to function as a broad-spectrum tumor suppressor. The full-length AIMP2 transcript consists of four exons, with a small section of the pre-mRNA undergoing alternative splicing to produce a variant (AIMP2-DX2) lacking the second exon. AIMP2-DX2 binds to FBP, TRAF2, and p53 similarly to AIMP2, but competes with AIMP2 for binding to these target proteins, thereby impairing its tumor-suppressive activity. AIMP2-DX2 is specifically expressed in a diverse range of cancer cells, including breast cancer, liver cancer, bone cancer, and stomach cancer. There is growing interest in AIMP2-DX2 as a promising biomarker for prognosis and diagnosis, with AIMP2-DX2 inhibition attracting significant interest as a potentially effective therapeutic approach for the treatment of lung, ovarian, prostate, and nasopharyngeal cancers.

• Microbiology and Biotechnology Letters
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• v.40 no.4
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• pp.348-355
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• 2012

In the present study, we investigated the overexpression and characterization of bovine pancreatic (bp)- DNase I in Saccharomyces cerevisiae and Pichia pastoris. The bp-DNase I gene was fused in frame with the GAL10 promoter, $MF{\alpha}$, and GAL7 terminator sequences, resulting in the plasmid, pGAL-$MF{\alpha}$-DNaseI (6.4 kb). Also, the bp-DNase I gene was fused in frame with the AOX1 promoter, $MF{\alpha}$, and AOX1 terminator sequences, resulting in the plasmid, pPEXI (8.8 kb). The recombinant plasmids, pGAL-$MF{\alpha}$-DNaseI and pPEXI were introduced into S. cerevisiae and P. pastoris host cells, respectively. When the transformed yeast cells were cultured at $30^{\circ}C$ for 48 h in galactose or methanol medium, bp-DNase I was overexpressed and the most of activity was found in the extracellular fraction. P. pastoris transformant activity showed 45.5 unit/mL in the culture medium at 48 h cultivation, whereas S. cerevisiae transformant revealed 37.7 unit/mL in the extracellular fraction at 48 h cultivation. The enzymatic characteristics, such as DNA cleavage and half life were investigated. Treatment of the recombinant DNase I from P. pastoris induced degradation of the calf thymus DNA within 1 minute, and this DNA degradation rate was higher than that of commercial bp-DNase I (SIGMA) and the recombinant DNase I from S. cerevisiae.

• Journal of the Korean Society of Tobacco Science
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• v.2 no.1
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• pp.1-7
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• 1980

Gel filtration column chromatography (Sephadex G-75), dialysis an d Brushite column chromatography were carried out to separate the brown pigmented macromolecule from water extracts of the cured leaf tobaccos. The two distinct macromolecules having different molecular weight were separated by the Sephadex column chromatography. Brushite also separated two different species of macromolecules which might have different electronic structures. According to the enzymatic degradation of protein in Burley and Hicks, chymotrypsin showed the best degradation ratio, ie., 16-30% in Burley and 38-57% in Hicks. Similar effect was observed with pepsin. However, very low effect of degradation was revealed with trypsin. The sample treated with the proteolytic enzymes revealed the disappearance of the first peak and the slight decrease of the 2nd peak height in the separation profile of Sephadex. After dialysis, the brown pigmented macromolecule was pyrolyzed at $300^{\circ}C$ and the strongly fluorescent components not identified before pyrolysis were detected with TLC separation. Absorption spectrum of these fluorescent compounds was monitored in benzene and the absorption maxima at 265nm and 275 nm were obtained. Considering absorption maxima and shape of the spectrum, those fluorescent compounds seem to be PAH derivatives.

• Mycobiology
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• v.37 no.1
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• pp.53-61
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• 2009

The process of biodegradation in lingo-cellulosic materials is critically relevant to biospheric carbon. The study of this natural process has largely involved laboratory investigations, focused primarily on the biodegradation and recycling of agricultural by-products, generally using basidiomycetes species. In order to collect super white rot fungi and evaluate its ability to degrade lingo-cellulosic material, 35 fungal strains, collected from forests, humus soil, livestock manure, and dead trees, were screened for enzyme activities and their potential to decolorize the commercially used Poly-R 478 dye. In the laccase enzymatic analysis chemical test, 33 white rot fungi and 2 brown rot fungi were identified. The degradation ability of polycyclic aromatic hydrocarbons (PAHs) according to the utilized environmental conditions was higher in the mushrooms grown in dead trees and fallen leaves than in the mushrooms grown in humus soil and livestock manure. Using Poly-R 478 dye to assess the PAH-degradation activity of the identified strains, four strains, including Agrocybe pediades, were selected. The activities of laccase, MnP, and Lip of the four strains with PAH-degrading ability were highest in Pleurotus incarnates. 87 fungal strains, collected from forests, humus soil, livestock manure, and dead trees, were screened for enzyme activities and their potential to decolorize the commercially used Poly-R 478 dye on solid media. Using Poly-R 478 dye to assess the PAHdegrading activity of the identified strains, it was determined that MKACC 51632 and 52492 strains evidenced superior activity in static and shaken liquid cultures. Subsequent screening on plates containing the polymeric dye poly R-478, the decolorization of which is correlated with lignin degradation, resulted in the selection of a strain of Coriolus versicolor, MKACC52492, for further study, primarily due to its rapid growth rate and profound ability to decolorize poly R-478 on solid media. Considering our findings using Poly-R 478 dye to evaluate the PAH-degrading activity of the identified strains, Coriolus versicolor, MKACC 52492 was selected as a favorable strain. Coriolus versicolor, which was collected from Mt. Yeogi in Suwon, was studied for the production of the lignin-modifying enzymes laccase, manganese-dependent peroxidase (MnP), and lignin peroxidase (LiP).

• Journal of Microbiology and Biotechnology
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• v.26 no.1
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• pp.9-19
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• 2016

Xylanases sourced from different bacteria have significantly different enzymatic properties. Therefore, studying xylanases from different bacteria is important to their applications in different fields. A potential xylanase degradation gene in Massilia was recently discovered through genomic sequencing. However, its xylanase activity remains unexplored. This paper is the first to report a xylanase (XynRBM26) belonging to the glycosyl hydrolase family (GH10) from the genus Massilia. The gene encodes a 383-residue polypeptide (XynRBM26) with the highest identity of 62% with the endoxylanase from uncultured bacterium BLR13. The XynRBM26 expressed in Escherichia coli BL21 is a monomer with a molecular mass of 45.0 kDa. According to enzymatic characteristic analysis, pH 5.5 is the most appropriate for XynRBM26, which could maintain more than 90% activity between pH 5.0 and 8.0. Moreover, XynRBM26 is stable at 37℃ and could maintain at least 96% activity after being placed at 37℃ for 1 h. This paper is the first to report that GH10 xylanase in an animal gastrointestinal tract (GIT) has salt tolerance, which could maintain 86% activity in 5 M NaCl. Under the optimum conditions, K_m, V_max, and k_cat of XynRBM26 to beechwood xylan are 9.49 mg/ml, 65.79 μmol/min/mg, and 47.34 /sec, respectively. Considering that XynRBM26 comes from an animal GIT, this xylanase has potential application in feedstuff. Moreover, XynRBM26 is applicable to high-salt food and seafood processing, as well as other high-salt environmental biotechnological fields, because of its high catalytic activity in high-concentration NaCl.