• Applied Biological Chemistry
• /
• v.23 no.1
• /
• pp.52-57
• /
• 1980

This study was conducted to clarify the mode of action and the positional specificity of Trichosporon cutaneum lipase during the course of hydrolysis of triolein and monoolein mixture by thin-layer chromatography. 1. The hydrolytic activity of the lipase to oleyl glycerides was in the order of triolein>diolein>monoolein. 2. Both of triolein and diolein were hydrolyzed by the lipase at high and almost the same rate. 3. The hydrolysis of monoolein by the lipase was very slow compared to the other two oleyl glycerides. 4. This lipase appeared to have a very low specificity toward the outer chains of triolein.

• Korean Journal of Microbiology
• /
• v.13 no.3
• /
• pp.85-90
• /
• 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 Environmental Biology
• /
• v.22 no.1
• /
• pp.184-191
• /
• 2004

To investigate bacteria with algalytic activities against Anabaena cylindrica when water blooming occurs and to study enzyme profiles associated with alga-lytic activity, various bacterial strains were isolated from surface waters and sediments in eutrophic lakes or reservoirs in Korea. Among 178 isolates, only nine isolates exhibited lytic abilities against A cylindrica on the agar plates, and then the isolate AK-13 was selected as the strongest in lysing the cyanobacterium A. cytindrica. The strain AK-13 was characterized and identified as Sinorhizobium sp. based on fatty acid methyl ether profiles and 16S rDNA sequence. According to the results of the enzyme assays, in the strain An-13 of Sinorhizobium sp., alginase, amylase, proteinase (caseinase and gelatinase), carboxymethyl-cellulase (CMCase), laminarinase, and lipase was produced, namely CMCase, laminarinase and protease were highly active. None of glycosidase was produced. Therefore, enzyme systems of Sinorhizobium sp. AK-13 were very complex to degrade cell walls of A. cylindrica. The peptidoglycans of A. cylindrica mat be hydrolyzed and metabolized to a range of easily utilizable monosaccharides or other low molecular weight organic substances by Sinorhizobium sp. AK-13.

• Asian-Australasian Journal of Animal Sciences
• /
• v.16 no.3
• /
• pp.389-393
• /
• 2003

Present study investigate the effect of enzyme supplementation, methods (applied to rumen or enzyme treated diet) compared with no enzyme diet, on rumen fermentation and apparent nutrient digestibility in a $3{\times}3$ Latin square design with three rumen cannulated Korean Native goats. In situ rumen degradation kinetics was studied in three rumen cannulated Holstein steers. Three diets were, no enzyme, 1% enzyme in rumen and 1% enzyme in diet. The enzyme was sprayed onto forage, and the forage: concentrate ratio was 30:70. Degradation kinetics was studied with three enzyme levels (0, 1 and 2%, w/w) and four pre-treatment times (0, 1, 12 and 24 h). Results suggested that enzyme application method did not affect rumen fermentation, ruminal enzyme activity and total tract apparent digestibility. Nutrient degradation rate and effective degradability of DM, NDF and ADF increased with increasing enzyme level and pre-treatment times. Degradation of nutrients was affected by enzymes levels or pre-treatment times. Therefore, it is probable that the improved degradation may be due to the supplemented exogenous hydrolytic enzymes under a certain condition.

• Korean Journal of Pharmacognosy
• /
• v.16 no.2
• /
• pp.99-104
• /
• 1985

To investigate a possible biological activity of iridoid glucosides, six compounds, aucubin, catalpol, gardenoside, geniposide, rehmannioside and swertiamarin, were studied in relation with their potential influences in RNA and protein biosyntheses in murine tumor cell, sarcoma 180, in vitro. Protein biosynthesis was slightly inhibited by aucubin, gardenoside and swertiamarin. Degree of inhibition of RNA biosynthesis by those iridoid appeared to be more sensitive than that of protein biosynthesis. When aucubin was pretreated with ${\beta}-glucosidase$ to produce its genin form and the sarcoma 180 cells were exposed to this aucubigenin, the protein and RNA biosyntheses in the cells were profoundly inhibited. The results indicate that a biologically active from of iridoid compounds is the hydrolytic products of glycoside, i.e. genin form. It is also suggested that sarcoma 180 cells used in the experiments appear to lack of ${\beta}-glucosidase$, since the inhibitory actions of iridoid glucosides were so slight that those glucosides were not hydrolysed by the enzyme to their genin forms.

• Journal of Korean Society of Water and Wastewater
• /
• v.17 no.4
• /
• pp.550-558
• /
• 2003

Digestion of primary sludge was conducted to evaluate the effects of reactor configuration using UAD, CUAD, TPAD, and semi-continuos CSTR. Highest VSS reduction and gas production were obtained in CUAD at all HRT. More efficient digestion was accomplished in upflow digesters compared to TPAD and CSTR. Higher thickening of solids in reactor and longer solids retention were main reasons for the enhanced digestion in CUAD and UAD. Performance based on the SRT of CUAD was nearly identical to that of UAD. However, those of TPAD and CSTR were lower than that of CUAD. Particulate and soluble organics in upflow reactors were well adsorbed due to secreted extracellular polymeric substances from the sludge granules. These might result in close proximity of microorganisms and substrates and enhanced hydrolysis. Additionally, diverse anaerobic microorganisms and neutral pH in upflow reactor could induce more activity of hydrolytic enzymes and sludge granules might offer lower thermodynamic energy state. While, excessive mixing in CSTR could break conglomerates of enzymes and substrates into fine particles, which resulted in lowered hydrolysis. Low pH level in acid fermenter of TPAD lowered hydrolysis of the particulate substrates.

• Journal of Microbiology and Biotechnology
• /
• v.20 no.10
• /
• pp.1415-1423
• /
• 2010

An extracellular xylanase was purified to homogeneity by sequential chromatography of Fomitopsis pinicola culture supernatants on a DEAE-Sepharose column, a gel filtration column, and then on a MonoQ column with fast protein liquid chromatography. The relative molecular mass of the F. pinicola xylanase was determined to be 58 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis and by size-exclusion chromatography, indicating that the enzyme is a monomer. The hydrolytic activity of the xylanase had a pH optimum of 4.5 and a temperature optimum of $70^{\circ}C$. The enzyme showed a $t_{1/2}$ value of 33 h at $70^{\circ}C$ and catalytic efficiency ($k_{cat}=77.4\;s^{-1}$, $k_{cat}/K_m$=22.7 mg/ml/s) for oatspelt xylan. Its internal amino acid sequences showed a significant homology with hydrolases from glycoside hydrolase (GH) family 10, indicating that the F. pinicola xylanase is a member of GH family 10.

• Journal of the Korean Society of Clothing and Textiles
• /
• v.24 no.2
• /
• pp.205-213
• /
• 2000

This study investigated the effect of mixing protease and lipase on detergency. The detergency of protein soiled, oil soiled and protein-oil soiled cloths and the relative hydrolytic activity of enzymes were examined. The protease-lipase added detergent solution was most effective for the removal of protein in protein-oil soiled cloths. This is because the lipase removed the protein that was physically bound to oil as well as the protease removed the protein. The protease added detergent solution was second effective, the lipase added detergent solution was third effective, and the detergent solution without protease and lipase was the least effective. The protease-lipase added detergent solution was also most effective in the oil removal from protein-oil soiled cloths. Unlike in protein removal, however, the protease added detergent solution was more effective in oil removal than the lipase added detergent solution. This is because the removal of oil bound to protein by protease was more effective than the removal of oil by lipase. In soiling-washing cycles, however, the effects of lipase increased, and as a result, the detergency of protease added detergent solution and the lipase added detergent solution became similar.

• Journal of Sericultural and Entomological Science
• /
• v.22 no.1
• /
• pp.46-51
• /
• 1980

The effects of foliar Spray of CCC [(2-Chloroethyl)-trimethyl-ammonium Chloride] on the growth of mulberry tree and the metabolic activities in the leaves were measured. The results of this experiment are summarized as follows; 1. Foliar application of CCC was not effective in increasing of leaf area, the fresh and dry weight of the leaves and height of shoot, but was effective in increasing of diameter of Shoot. 2. Chlorophyll Content was generally increased in all treated leaves 3. All the treated leaves were lower in GOT and GPT activity than control leaves. 4. The activities of hydrolytic reducing Sugar in the mulberry leaves infiltrated Sucrose were lower than those of the control in all treated leaves, but the activities on Synthetic non-reducing Sugar in the mulberry leaves infiltrated glucose were higher than those of control in all treated leaves.

• Korean Journal of Food Science and Technology
• /
• v.54 no.1
• /
• pp.88-93
• /
• 2022

In this study, silkworms fed Cudrania tricuspidata leaves were powdered, and hydrolytic enzymes, including viscozyme, papain, and flavourzyme, were added to verify the functionality of the different mixtures. In the general component analysis, the C. tricuspidata silkworm (CS) group exhibited higher crude protein and ash content than did the other groups, and the enzyme-treated groups exhibited higher carbohydrate content than the CS group. The DPPH and ABTS radical scavenging activities were significantly higher in the CS treated with viscozyme (CSV) and the CS treated with viscozyme/flavourzyme (CSVF) than in the other groups, with the CSV group showing the highest reducing power. ACE inhibitory activity was significantly higher in the CS treated with visocozyme/papain (CSVP) than in the CS group. In conclusion, rather than using powdered silkworms fed C. tricuspidata leaves, it would be more effective to use hydrolysates from C. tricuspidata silkworms as raw materials for functional foods.