• The Korean Journal of Food And Nutrition
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• v.36 no.1
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• pp.42-49
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• 2023

To enhance the efficacy of Abeliophyllum distichum leaves, extracts were prepared using different solvents for hydrolytic enzyme-treated Abeliophyllum distichum leaves. Physicochemical quality and antioxidant activity were measured. Soluble solids, reducing sugar, ascorbic acid, flavonoids, and polyphenols contents showed the lowest values in the control without enzyme treatment. However, they showed high contents in ethanol extract. In the case of enzyme treatment, their values were higher than those of the control. In particular, verbascoside content increased about 220 times more than that of the control group when treated with enzymes and extracted with 50% ethanol. pH was lowered upon enzymatic treatment. Regarding DPPH radical scavenging activity, for enzyme-free, 25% ethanol extract showed the highest activity among extracts with different solvents. For cellulase and pectinase-treated leaves, water extract showed the highest DPPH radical scavenging activity among extracts with different solvents. For leaves treated with enzyme combination, 50% ethanol extract showed the highest DPPH radical scavenging activity among extracts with different solvents. Regarding ABTS radical scavenging activity, it was generally higher in the 50% ethanol extract than in the water extract and 25% ethanol extract. In particular, verbascoside content was increased when the extract was prepared by co-treatment with enzymes and 50% ethanol.

• Korean Journal of Microbiology
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• v.45 no.1
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• pp.32-40
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• 2009

To understand contribution of thermophilic microorganisms in decomposition of litter deposits on shore of lakes, we surveyed a lakeshore litter deposit for bacteria growing at $60^{\circ}C$. Ten thermophilic isolates were selected for in-depth characterization, based on their high capacity to degrade high molecular weight organic compounds. Based on phylogenetic analysis on their 16S rRNA gene sequences, all isolates were identified as Geobacillus. The optimal growth temperature and pH of the strains ranged $55{\sim}60^{\circ}C$ and 6.0${\sim}$8.0, respectively. Salinity was inhibitory to the growth of the isolates, showing marked decrease of growth rates at 3% salinity. Based on activities of hydrolytic enzymes and profiles of carbohydrate utilization (determined by API 50 CHB kit), three G. stearothermophilus strains showed patterns clearly distinctive from other isolates. Two G. kaustophilus strains also demonstrated distinctiveness in their metabolic pattern and ecological parameters. However, ecological and metabolic profiles of the other five isolates were more variable and showed some degree of digression from their phylogenetic classification. Therefore, it could be concluded that endospore-forming thermophilic bacteria in lakeshore litter deposits contribute to degradation of organic materials with diverse ecological niches while having successions similar to microbial flora in compost. We propose that the thermophilic isolates and/or their thermo-tolerant enzymes can be applied to industrial processes as appropriate mixtures.

• Journal of Microbiology and Biotechnology
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• v.8 no.3
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• pp.197-202
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• 1998

Aliphatic alkenals having 6 to 13 carbons were evaluated for antifungal activity against Saccharomyces cerevisiae. The activity was gradually increased with chain length, e.g., (E)-2-decenal and (E)-2-undecenal exhibited maximum potency, while (E)-2-dodecenal and (E)-2-tridecenal were completely inactive. Alkenals showed increasing inhibitory activity with chain length, as in the case of antifungal activity, towards glucose-induced medium acidification by the plasma membrane $H^+$-ATPase of S. cerevisiae. The group including (E)-2-nonenal, (E)-2-decenal, and (E)-2-undecenal exhibited maximum potency, but the potency of (E)-2-dodecenal and (E)-2-tridecenal demonstrated a sudden drop with respect to the former group. (E)-2-Nonenal revealed dose-responsive inhibition to the medium acidification and inhibited over 90% at a concentration of 1.25 mM ($175.3{\mu}g$/ml). In contrast to (E)-2-undecenal whose inhibitory efficiency increased with incubation time, inhibition by (E)-2-dodecenal was reversed with time. Of the tested alkenals, (E)-2-heptenal and (E)-2-octenal most highly inhibited ATP hydrolytic activity by the plasma membrane $H^+$ ATPase, while (E)-2-heptenal at 10 mM ($1121.8{\mu}g$/ml) showed an inhibitory efficacy of 93.2%.

• 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.

• Korean Journal of Microbiology
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• v.20 no.4
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• pp.201-209
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• 1982

An enzyme, named GTP cyclohydorlase, that catalizes the hydrolytic removal of carbon No.S of GTP has been partially purified from extracts of Pseudomonas putida (IAM 1506). The enzyme exists in two molecuar weight forms : a high molecular weight form (150,000) and a low molecular weight from (40,000). The high molecular weight form has been purified 25-fold. Some of the properties of the enzyme are as follows : It functions optimally at pH8.0, and at $52^{\circ}C$. The Km value for GTP is $20{\mu}M$. Divalent cations $(Cd^{2+}\;and\;Hg^{2+})$ 2+/) at a concentration of 5mM inhibit completely the enzyme activity. No metal ion including $Mg^{2+}$ is needed for the catalysis. The enzyme is heat labile ; its half at $57^{\circ}C$ is 1.5 min. Of a number of nucleotides tested, only GDP was used to any extent as substrbte in place of GTP. One of the products of the enzyme is determined to be a dihydro-neopterin compound.

• Journal of the Korean Society of Clothing and Textiles
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• v.35 no.6
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• pp.670-677
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• 2011

This study is to optimize the enzymatic processing conditions of Polylactic Acid (PLA) fiber using lipase from Porcine pancreas as an environmental technology. Hydrolytic activity dependent on pH, temperature, enzyme concentration, and treatment time, and structural change of PLA fiber were evaluated. The PLA fiber hydrolysis by lipase was maximized at 50% (o.w.f) lipase concentration $50^{\circ}C$ for 120 minutes under pH 8.5. There was a change of the protein absorbance in the treatment solution before and after the lipase treatment. In addition, there was no substantial change in the molecular and crystalline structures of PLA by lipase treatment as confirmed by DSC, XRD, and FT-IR.

• Journal of Microbiology and Biotechnology
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• v.16 no.12
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• pp.1897-1903
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• 2006

In order to investigate the functions of the C-terminal region of chitinase ChiCW of Bacillus cereus 28-9, a C-terminal truncated enzyme, ChiCW$\Delta$FC, was expressed in Escherichia coli and purified to homogeneity for biochemical characterization. Compared with ChiCW, ChiCW$\Delta$FC exhibited higher chitinase activity at high temperature and pH, but expressed lower hydrolytic and binding activities toward insoluble substrates. In addition, kinetic properties indicated that ChiCW$\Delta$MC hydrolyzed oligomeric and polymeric substrates less efficiently than ChiCW. These results suggest that the C-terminal region of ChiCW plays important roles in substrate binding and hydrolysis of chitin. In addition, the biological meaning of C-terminal proteolytic modification of ChiCW is discussed.

• Microbiology and Biotechnology Letters
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• v.25 no.2
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• pp.218-223
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• 1997

For the utilization of animal blood produced in slaughter for the cultivation of lactic acid bacteria, the nitrogen sources in a complex(MRS) medium were replaced by blood plasma proteins. Focusing the purpose on the industrial production of a probiotics, the hydrolytic activities of three industrially applicable proteases were compared for the effective digestion of the proteins, and Alcalase(the product of Novo Nordisk) was selected with comparatively high activity. The growth of Streptococcus thermophilus KCCM12020 was best among the four strains of lactic acid bacteria tested. With Alcalase-digested proteins in the medium, the growth rates and the final cell concentrations were higher than those with non-digested proteins. The cell mass produced in the medium containing blood proteins as nitrogen sources, $2.5{\times}10^9$ CFU/ml, was significantly high and about 70% of that in MRS medium, showing a great possibility for the utilization of animal blood proteins as economic nitrogen sources in the production of cell mass of lactic acid bacteria.

• Journal of Marine Bioscience and Biotechnology
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• v.2 no.1
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• pp.11-22
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• 2007

This aims to review natural products transformed by mimic intestinal metabolisms with microorganisms and hydrolytic enzymes, which exhibit enforced biological activity, higher extraction yield and identification of active components. In the process, transformation to the smaller active compounds with enzymes and microbes mimics the pharmacological action of natural products by intestinal bacteria. In order to establish conditions for the fermentation and enzyme reaction, it is required to choose several natural products for biotransformation and investigate the optimal conditions for the fermentation or the enzyme reaction such as composition, temperature, pH, inoculum, and cultivation time. It is expected an increase of the internal absorption of the active materials without regard to the intestinal microbes or its ability through biosynthesis of the active materials by the microbes and enzymes. And this techniques can be applied to biotransformation of natural products such as sesaminol, resveratrol, 1-deoxy nojirimycin, naringenin, quercetin, and baicalin and to the metabolism study using the animal model.

• Fisheries and Aquatic Sciences
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• v.2 no.2
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• pp.218-225
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• 1999

A protease without tryptic and chymotryptic activities was purified from the hepatopancreas of shrimp, Penaeus orientalis, using Q-Sepharose ionic exchange, benzamidine Sepharose-6B affinity, Mono-Q, and gel chromatography. Molecular weight (M.W.) of the protease was estimated to be 27kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS­PAGE). The amino acid composition of the protease was different from that of protease from P. japonicus or trypsin from P. orientalis. The protease was completely inhibited by benzamidine, $N\alpha-p-tosyl-L-lysine$ chloromethyl ketone (TLCK), and phenylmethylsulfonyl fluoride (PMSF) and was not affected by leupeptin, pepstatin, N-tosyl-L-phenylalanine chloromethyl ketone (TPCK), iodoacetate, and ethylenediamine tetra acetate (EDTA). The enzyme did not have any activity against Na-benzoyl-DL-arginine p-nitroanilide (BAPNA) or N-benzoyl-L-tyrosine ethyl ester (BTEE) which are specific substrates of trypsin and chymotrypsin, respectively. However, the protease showed hydrolytic activity for a carboxyl terminal of Tyr, Trp, Phe, Glu, and Cys.