• Korean Journal of Environmental Biology
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• v.22 no.1
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• pp.184-191
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• 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.

• Korean Journal of Microbiology
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• v.36 no.1
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• pp.14-19
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• 2000

Algal lytic enzyme, an extracellular enzyme, was purified from the culture filtrate of Penicillium oxalicum(HCLF-34) by ultrafiltration, gel filtration chromatography, and anion exchange chromatography. The enzyme has a molecular mass of approximately 22 kDa, an it is a monomer by renaturation SDS-PAGE. The amino acid sequences of the enzyme was revealed to be NH2-Glu-Ser-Tyr-Ser-Ser-Asn-Ala-Ala-Gly-Ala-Val-Leu-Ile---, had about 84% identity with the mature light chain of aspergillopepsin II precursor and 81% identity with the mature protein of the acid proteinase EapC precursor.

• KSBB Journal
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• v.24 no.6
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• pp.579-583
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• 2009

The effects of cell lytic enzyme treatment on total phenolic content, antioxidant and antityrosinase activities of lotus leaf were investigated. The dried lotus leaves were hydroyzed by cell lytic enzymes such as Promozyme, Ceremix, Pectinex, Ultraflo, Celluclast, Pentopan, Tunicase, Viscozyme at their optimum pHs (pH 5-8) at $50^{\circ}C$ for 4 hrs. Depending on the enzymes used, total phenolic compounds content was measured as $1,079-1,476{\mu}g$/mL, and antioxidant activities and whitening activities were increased by 5~10% and 20%, respectively Among the tested hydrolytic enzymes, Promozyme (pullulanase) was selected as the most suitable enzyme for the extraction of total polyphenol from lotus leaf. The optimal dosage of Promozyme were found to be 1-2% (w/w). By Promozyme treatment, total phenolic compounds content of the lotus extract significantly increased compared to the extraction without enzyme treatment.

• Korean Journal of Microbiology
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• v.21 no.4
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• pp.213-220
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• 1983

Conditions for isolation of protoplasts from conidiospores of Trichoderma koningii ATCC 26113 were tested. Maximum production of conidial protoplasts was obtained by preincubation of conidiospores on liquid minimal medium for 8 1/2 hrs. and by reaction with cell wall lytic enzyme for 3 hrs. Among effective cell wall lytic enzymes (Driselase, p-Glucuronidase, Novozyme and Zymolyase), Driselase was the most effective one on the production of conidial protoplasts. The production of conidial protoplasts was also enhanced by addition of 2-Deoxy-D-Glucose $(25{\mu}g/ml)$ into liquid minimal medium. Over 70% of the initial swollen conidia, preincubated in liquid minimal medium supplemented with 2-Deoxy-D-Glucose $(25{\mu}g/ml)$, were converted to protoplasts by incubation with 2% (w/v) commercial lytic enzyme Driselase at $28^{\circ}C$ for 3 hrs. The reversion frequency of the conidial protoplasts was about 30 times (25-50%) higher than that of mycelial protoplasts (0.6-1.3%).

• Journal of Microbiology and Biotechnology
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• v.5 no.4
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• pp.206-212
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• 1995

A strain BL-29, which produces a extracellular lytic enzyme on E. coli was isolated from the soil. The strain was identified as belonging to the genus Bacillus sp. The lytic enzyme was purified to homogeneity by ion exchange chromatography and gel filtration. Specific activity of the purified enzyme was 28, 850 U/mg protein and yield of the enzyme was 5$%$. The purified enzyme showed a single band on SDS-PAGE and its molecular weight was estimated to be 31, 000 by SDS-polyacrylamide gel electrophoresis and gel filtration column chromatography. The optimum temperature and pH were $55^{\circ}C$ and pH 10.0, respectively. The enzyme was stable at $45^{\circ}C$ but enzyme activity was reduced by up to 50$%$ when the temperature was raised to $55^{\circ}C$ for 15 min. Stable range of pH was from 5.0 to 11.0. but Enzyme activity was inhibited by lead-acetate, mercuric chloride, ethylene glycol-bis-[$\beta$-aminoethyl ether]-N, N, $N^1, $N^1$-tetraacetic acid (EGTA), and ethylenediamine tetraacetic acid (EDTA), but not affected considerably by treatment with other chemical reagents.

• Journal of Applied Biological Chemistry
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• v.63 no.4
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• pp.291-295
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• 2020

In order to increase the utilization of defatted sesame meal (DSM), a by-product of sesame oil production, the conditions of extraction of insoluble proteins from DSM by enzyme treatment were investigated. As a result of comparing the treatment results of proteolytic enzymes Alcalase, Flavorzyme, Neutrase, and Protamex with control, Protamex was effective in increasing the total solid and protein content. At the reaction conditions of Protamex (50 ℃, pH 6.0), the dosage of enzymes was appropriate for 1% of DSM and 3 h of enzyme reaction time. To improve the efficiency of enzymatic treatment, the protein content extracted increased as the heat treatment temperature increased, and slightly increased above 110 ℃. As a result of investigating the effect of the combination treatment of cell lytic enzyme (Tunicase) and protease (Protamex) on protein solubilization, it was most effective to treat the cell lytic enzyme after processing the protease. After heat treatment (110 ℃, 10 min), sequential treatment of Protamex and Tunicase increased the protein content by about 3.5 times (9.85→35.58 mg/mL) of the non-heated control and 2.2 times (15.83→35.58 mg/mL) of the heat treated control.

• Korean Journal of Food Science and Technology
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• v.11 no.4
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• pp.242-248
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• 1979

To detect proper lytic assay conditions of the crude zumolyase from Arthrobacter luteus, effets of the various factors involved in the lytic system of Sacchromyces sake cultured with shaking in the malt extracts medium were investigated. The results are summarized as follows : 1. The susceptibilities of viable cells of S. sake from logarithmic growth phase to the lytic enzmye were much greater than those of the cells in lag and stationary phases. The cells cultured for 18 hr were the most susceptible to the enzyme. 2. Lytic activity of the enzyme toward the viable cells of S. sake was very low. It was, however, enhanced 4 folds of more by the pretreatment of the cells with 0.05 M sodium sulfite. 3. Lytic activity of the enzyme toward commercial baker's yeast cells was negligible, and the effect of sodium sulfite on the lysis of the cells also was nothing but a little. 4. The lyophilized cells of the baker's yeast showed more susceptibility to the lytic enzyme than viable cells of the yeast. No definite effect of sodium sulfite on the lysis of the lyophilized cells, however, was observed either baker's yeast of S. sake. 5. It appeared that the relationship between the reaction rate and the enzyme concentration on the lysis of the yeast cell walls followed enzyme kinetic theory, but one between the reaction rate and concentration of the yeast cells as substrates showed different pattern from that in enzyme kinetic theory. 6. After the preparation of crude zymolyase was kept at $7^[\circ}C$ for 10 days in the 0.05 M phosphate buffer, pH 7.5, the remainning lytic activity was about 80 %.

• Biotechnology and Bioprocess Engineering:BBE
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• v.11 no.5
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• pp.382-390
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• 2006

Various microorganisms were isolated from the surface waters and sediments of eutrophic lakes and reservoirs in Korea to enable an investigation of bacteria having algal lytic activities against Anabaena flos-aquae when water blooming occurs and to study enzyme profiles of algal lytic bacteria. Two bacterial strains, AFK-07 and AFK-13, were cultured, characterized and identified as Acinetobacter johnsonii and Sinorhizobium sp., respectively. The A. johnsonii AFK-07 exhibited a high level of degradatory activities against A. flos-aquae, and produced alginase, caseinase, lipase, fucodian hydrolase, and laminarinase. Moreover, many kinds of glycosidase, such as ${\beta}-galactosidase,\;{\beta}-glucosidase,\;{\beta}-glucosaminidase,\;and\; {\beta}-xylosidase$, which hydrolyzed ${\beta}-O-glycosidic$ bonds, were found in cell-free extracts of A. johnsonii AFK-07. Other glycosidases such as ${\alpha}-galactosidase,\;{\alpha}-N-Ac-galactosidase,\;{\alpha}-mannosidase,\; and\;{\alpha}-L-fucosidase$, which cleave ${\alpha}-O-glycosidic$ bonds, were not identified in AFK-07. In the Sinorhizobium sp. AFK-13, the enzymes alginase, amylase, proteinase (caseinase and gelatinase), carboxymethyl-cellulase (CMCase), laminarinase, and lipase were notable. No glycosidase was produced in the AFK-13 strain. Therefore, the enzyme system of A. johnsonii AFK-07 had a more complex mechanism in place to degrade the cyanobacteria cell walls than did the enzyme system of Sinorhizobium sp. AFK-13. The polysaccharides or the peptidoglycans of A. flos-aquae may be hydrolyzed and metabolized to a range of easily utilized monosaccharides or other low molecular weight organic substances by strain AFK-07 of. A. johnsonii, while the products of polysaccharide degradation or peptidoglycans were more likely to be utilized by Sinorhizobium sp. AFK-13. These bacterial interactions may offer an alternative effective approach to controlling the water choking effects of summer blooms affecting our lakes and reservoirs.

• The Journal of Korean Academy of Prosthodontics
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• v.31 no.1
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• pp.28-38
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• 1993

For the purpose of evaluating the cleansing efficiency against Candida albicans detected frequently in patients with denture stomatitis, two denture cleansers with or without enzymes were studied under the same conditions. The results were as fellows: 1. Enzyme-contain denture cleanser was showed more Candida albicans lytic ability than non-enzyme-contained denture cleanser. 2. It was observed that Candida albicans lytic activity in further diluted manufacturerers' recommended concentration was decreased. 3. In fungicidal test, the enzyme-contained denture cleanser sterilized Candida albicans, and the non-enzyme-contained denture cleanser did not sterilize Candida albicans. 4. Sterilizing time of Candid albicans was needed for at least 60 minutes in enzyme-contained denture cleanser solution which was diluted with manufacturerers' recommended concentrations., and was needed for more times with further diluted manufacturerers' recommended concentrations. 5. In vitro growth test of Candida albicans on acrylic resin surface, the only enzyme-contained denture cleanser inhibited growth of Candida albicans, and it was observed that inhibiton ability of growth of Candida albicans on arrylic resin surface was decreased in further diluted manufacturerers' recommended concentrations.

• The Korean Journal of Mycology
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• v.14 no.4
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• pp.273-280
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• 1986

The degree of autolysis and lytic enzyme production in the culture filtrate of Rhizopus oryzae was investigated. The formation of protoplast by using autolytic enzymes from Rh. oryzae was also attempted. Protoplasts were liberated from Rh. oryzae mycelium by lytic enzymes present in autolytic-phase culture filtrate. Maximum release of chitosanase and proteolytic enzyme into culture filtrate during autolysis was corresponded to maximum protoplast-liberating activity. High yields of protoplasts were obtained from 10 hr-age of Rh. oryzae mycelium with 0.5 M mannitol as osmotic stabilizer. The optimum temperature and pH for mycelium digestion were $25{\sim}30^{\circ}C$ and $6.0{\sim}6.5$ respectively. The mycelium of the 18 hours cultures were treated with autolytic enzyme in same volume of osmotic stabilizer at $30^{\circ}C$ for 5 hours and then it was confirmed by scanning electoron microscope that protoplast were produced beside the digesting cell wall of the fungi.