• Korean Journal of Environmental Agriculture
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• v.15 no.1
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• pp.105-115
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• 1996

In this paper, we reviewed the degradation factors of diazinon which was known to be easily degraded by soil microorganisms and lost of its activity. Under submerged soil condition, the contribution of microorganisms to diazinon degradation was about 40% and these microorganisms preferred soil humus as substrates to diazinon itself. The effect of monooxygenase activity in submerged soil was more important than esterase activity on diazinon degradation and these enzymes were inhibited by several chemicals such as piperonyl butoxide(PBO), EPN and tricyclazole. From these results, new formulation type of diazinon (PBO and triphenyl phosphate were added to commercial diazinon formulation by 0.1% respectively.) and diazinon mixture formulation (diazinon was mixed with EPN, tricyclazole and carbofuran in equal amount) were prepared. The new formulation type of diazinon showed better insecticidal activity by 12% and more delayed diazinon degradation in ten days than commercial diazinon.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.37 no.3
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• pp.17-22
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• 2005

The cleaning efficiency of papermaking felt which is contaminated with fiber fines and various micro-materials was investigated and compared between the application of enzyme and commercial detergent. It was found that the cleaning efficiency by the treatment of acidic-based detergent was more efficient than that of alkaline-based one in the conventional commercial detergent. it was also observed that the treatment design of first acidic-based detergent treatment to second alkaline-based detergent procedure was better in the cleaning efficiency, compared to alkaline based-to-acidic based one. The cleaning property of felt with enzyme was resulted in good cleaning efficiency, without any addition of surfactant. Especially, the enzyme treatment under alkaline condition (pH 10) showed a better cleaning result than that under acidic condition(pH 5). The addition of nonionic surfactant to the enzyme increased the cleaning efficiency of felt and decreased the cationic demand of wastewater. These results showed more favour than the application of conventional commercial detergent.

• Journal of Plant Biotechnology
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• v.29 no.3
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• pp.199-207
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• 2002

The tropane alkaloids hyoscyamine (its racemic form being atropine) and scopolamine are used medicinally as anticholinergic agents that act on the parasympathetic nerve system. Because they differ in their actions on the central nervous system, currently there is a 10-fold higher commercial demand for scopolamine, in the N-butylbromide form, than there is for hyoscyamine and atropine combined. Several solanaceous species have been used as the commercial sources of these alkaloids, but the scopolamine contents in these plants often are much lower than those of hyoscyamine. For this reason there has been long-standing interest in increasing the scopolamine contents of cultivated medicinal plants. Naturally occurring and artificial interspecific hybrids of Duboisia have high scopolamine contents and are cultivated as a commercial source of scopolamine in Australia and other countries. Anther culture combined with conventional interspecific hybridization also has been used to breed high scopolamine-containing plants in the genera Datura and Hyoscyamus, but without much success. The use of recombinant DNA technology for the manipulation of metabolic processes in cells promises to provide important contributions to basic science, agriculture, and medicine. In this review, I introduce on the enzymes and genes involved in tropane alkaloid biosynthesis and current progress in metabolic engineering approaches for tropane alkaloid, especially scopolamine, production.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.42 no.6
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• pp.537-544
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• 2009

This study was conducted to improve yield and functional properties of autoclave-treated salmon frame extracts (SFETA) using commercial enzymes (Alcalase 2.4 L FG, Flavourzyme 500 MG, Neutrase 0.8 L and Protamex 1.5 MG). Yield and angiotensin I converting enzyme (ACE) inhibitory activity of all enzymatic hydrolysates improved compared to those of control (undigested extracts), which were the highest in hydrolysates incubated with Protamex 1.5 MG for 4 hrs (P4-treated hydrolysates) and 2 hrs (P2-treated hydrolysates), respectively. However, antioxidant activities of all enzymatic hydrolysates showed less than 29%. According to the trichloroacetic acid soluble-N, volatile component intensity and sensory evaluation, when compared to control, taste of P4-treated hydrolysates improved, while its fish odor strongly smelt. Therefore, for efficient use of P4-hydrolysates, the fish odor should be improved by Maillard reaction of extracts or pre-treatment of salmon frame.

• Asian-Australasian Journal of Animal Sciences
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• v.17 no.5
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• pp.712-718
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• 2004

This study was carried out to separate the calcium-binding protein derived from enzymatic hydrolysates of cheese whey protein. CWPs (cheese whey protein) heated for 10 min at $100^{\circ}C$ were hydrolyzed by trypsin, papain W-40, protease S, neutrase 1.5 and pepsin, and then properties of hydrolysates, separation of calcium-binding protein and analysis of calcium-binding ability were investigated. The DH (degree of hydrolysis) and NPN (non protein nitrogen) of heated-CWP hydrolysates by commercial enzymes were higher in trypsin than those of other commercial enzymes. In the result of SDS-PAGE (sodium dodecyl sulphate polyacrylamide gel electrophoresis), $\beta$-LG and $\alpha$-LA in trypsin hydrolysates were almost eliminated and the molecular weight of peptides derived from trypsin hydrolysates were smaller than 7 kDa. In the RP-HPLC (reverse phase HPLC) analysis, $\alpha$-LA was mostly eliminated, but $\beta$-LG was not affected by heat treatment and the RP-HPLC patterns of trypsin hydrolysates were similar to those of SDS-PAGE. In ion exchange chromatography, trypsin hydrolysates were shown to peak from 0.25 M NaCl and 0.5 M NaCl, and calcium-binding ability is associated with the large peak, which was eluted at a 0.25 M NaCl gradient concentration. Based on the results of this experiment, heated-CWP hydrolysates by trypsin were shown to have calcium-binding ability.

• Food Science of Animal Resources
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• v.35 no.4
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• pp.533-540
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• 2015

The aim of this study was to investigate the effects of aqueous extract from Sarcodon aspratus on tenderization of the bovine longissimus dorsi muscles in comparison with commercial proteolytic enzymes. Furthermore, meat quality and muscle protein degradation were examined. We marinated meat with 2% Sarcodon aspratus extract, 2% kiwi extract, and 0.2% papain. Beef chunks (3×3×3 cm³) were marinated with distilled water (control), Sarcodon aspratus extract (T1), kiwi extract (T2) or papain (T3) for 48 h at 4℃. There were no significant differences in muscle pH and lightness between control and treated samples. T1 had the lowest redness (p<0.01), and higher cooking loss and water holding capacity than control and T2 (p<0.05). T1 and T3 exhibited lower shear force values than control (p<0.05). Total protein solubility did not differ significantly between T1 and control, but T1 had less myofibrillar protein solubility than control and T2 (p<0.001). The degradation of myosin heavy chain in T1 and T3 was observed. This degradation of myofibrillar protein suggests that Sarcodon aspratus extract could influence tenderization. These results show that aqueous extract of Sarcodon aspratus extract actively affect the tenderness of the bovine longissimus dorsi muscle.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1190-1195
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• 2004

In recent years, there has been an intensive research on decolorization of dye and textile wastewater by various fungal strains. In this study, the decolorization ability of three commercial dyes, acid yellow 99, acid blue 350, and acid red 114, were investigated using 10 fungal strains. Among the fungal strains tested, Trametes versicolor KCTC 16781 completely decolorized all dyes in both solid and liquid experiments, and was also able to decolorize the mixture of those three dyes in liquid experiments. The secretion of the ligninolytic enzymes into the extracellular medium during decolorization by T versicolor KCTC 16781 was also studied. No lignin peroxidase activity was detected, and manganese peroxidase and laccase activities were investigated.

• Korean Journal of Microbiology
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• v.13 no.3
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• pp.85-90
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• 1975

Crude cellulases freshly prepared from cultures of Aspergillus niger, Prnicillum motatum, Trichoderma vride 16273 and Trichoderma viride 16374 were assayed on 4 different substrates including Na-CMC, cellulose powder, starch and sucrose. Enzyme prepared from A. niger contained highly active hydrolytic enzymes of the 4 substrates assayed. P. notatum [yielded relatively lower amount of cellulase but the extracts were also highly reactive on starch and sucrose. Trichoderma viride 16274 yielded very little cellulase and invertase, but the extracts showed a high degree of amylase activity. Trichoderma viride 16374, however, yielded collulase comparable to that of Penicillium notatum, but lower activities of amylase and invertase were seen. Commercial cellulases prepared from Penicillium notatum (cellulase[K]) and Trichoderma viride(cellulase[J]) indicated enzyme activities closely parallel to the crude enzymes freshly prepared from fungus cultures. The optimum pH's of cellulolytic activities of cellulase[K] and cellulase[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase[K] and cellualse[J] were 4.0 and 5.0 respectively. The optimum temperatures of the cellulolytic activities of cellulase [K] and cellulase [J] were $60{\circ}C$ and $50{\circ}C$ respectively. Assuming the average molecular weight of Na-CMC is about 115,000, the Km values of cellulase [K] and cellulase[J] were found to be $3.3{\times}10^{-5}/nM$ and $3.3{\times}10^{-4}/nM$ respectively.

• Korean Journal of Veterinary Research
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• v.39 no.1
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• pp.104-110
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• 1999

Field infectious bursal disease viruses (IBDVs) were isolated from IBDV-suspected commercial chickens. The variable region in VP2 gene of six Korean IBDV isolates (K-IBDVs) and IBD vaccines was examined using the reverse transcriptase / polymerase chain reaction-restriction fragment length polymorphism (RT/PCR-RFLP) assay. With all K-IBDVs and vaccine IBDVs, a 474-bp fragment of the VP2 gene was amplified and tested with various restriction enzymes. Restriction enzymes BstNI and StyI differentiated K-IBDV isolates and IBD vaccines into four groups. Restriction enzyme profiles of K-IBDV isolates were different from them of IBD vaccines. K-IBDV isolates except for 310 isolate had specific SspI and TaqI recognition sites, which were recognized in highly virulent IBDVs, but IBD vaccines had no those sites. This study showed that RT/PCR-RFLP assay was thought to be valuable tool for differentiation of IBDVs and identification of highly virulent IBDV.

• Food Science of Animal Resources
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• v.21 no.3
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• pp.256-264
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• 2001

Pyrolysis/GC-mass spectrometry(Hewlet-Packard 5890GC/mass selective detector, 5971 BMSD), interfaced to a CDS Pyroprobe 1500 was optimized for rapid analysis of flavour compounds in Cheddar cheese. Twenty flavour compounds, including aldehydes(4), ketones(4), fatty acids(10), alcohol(1), and hydrocarbon(1), were identified from Cheddar cheeses. In total, Twenty-three flavour compounds aldehydes(2), ketones(8), alcohols(3), fatty acids(7), lactone(1), benzene derivative(1) and amide(1) were identified from two samples of accelerated-ripened Cheddar cheese treated with the proteolytic enzymes of Lactobacillus casei LGY. In total, Twenty-one flavour compounds; aldehydes(2), ketones(5), alcohols(2), fatty acids(11), and lactone(1) were identified from enzyme-modified cheese(EMC) treated with the combination of the proteolytic enzymes of Lactobacillus casei LGY and commercial endopeptidase or lipase. However, All the flavour compounds identified by pyrolysis/GC/MS in samples of ARC and EMC were not determined whether they are recognized as typical Cheddar flavour or not. More studies were requested on the development of methods for a rapid and convienent analysis of dairy fermented products using pyrolysis/GC-mass spectrometry.