• Microbiology and Biotechnology Letters
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• v.14 no.6
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• pp.467-471
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• 1986

Yeast cell wall lytic enzyme was purified from Fusarium moniliforme by ammonium sulfate fractionation and gel column chromatography. The lytic activity was found to consist of three enzyme activities which were resolved on Sephadex G-100. The first peak on chromatogram exhibited proteolytic, lytic and laminarinase activities, and the second had both lytic and laminarinase activities, whereas the third peak was shown to contain lytic activity only. Three enzyme activities showed the synergistic effect and reducing agents accelerated the yeast roil wall lysis. This indicates that lytic, proteolytic and laminarinase activity acted cooperatively in the lysis of intact cells. Tannic acid precipitate of crude enzyme constituted of three enzyme activities had a high lytic activity on viable yeast cell and has proved useful in yeast protoplast formation.

• Journal of Microbiology and Biotechnology
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• v.16 no.10
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• pp.1613-1621
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• 2006

Isolation and identification of algal lytic bacteria were carried out. Nine strains of algal lytic bacteria were isolated by the double-layer method using Anabaena flos-aquae as a sole nutrient. The isolate, AFK-13, showing the highest algal lytic activity was identified as Sinorhizobium kostiense based on the l6S rDNA sequence. The algal lytic experiments of the culture supernatants of AFK-13 demonstrated that the bacterial cell growth reached a maximum at 36-h culture, but the supernatant of 72-h culture exhibited the highest activity. Components among the extracellular products in the crude enzyme of the supernatant from S. kostiense AFK-13 culture were responsible for degradation of cell walls of Anabaena flos-aquae. Algal lytic assay tests of the culture supernatants suggest that the main substances for algal lytic activity could be proteinaceous. The activity of glucosidase was observed highly by polysaccharolytic analysis using the crude enzyme from S. kostiense AFK-13, whereas activities of galactosidase, mannosidase, rhamnosidase, and arabinosidase were also detected in low levels. The molecular weights (MW) of ${\alpha}-\;and\;{\beta}$-glucosidases were estimated to be approximately 50-100 kDa by the ultrafiltration method.

• Korean Journal of Food Science and Technology
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• v.9 no.2
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• pp.97-105
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• 1977

1) In order to obtain a microbial strain having a strong yeast cell wall lytic activity, about 156 isolates capable of forming clear zones on baker's yeast-peptone-bouillon agar plate were obtained from soil, mud and water samples and a strain K-42 with the highest lytic activity was identified as Bacillus circulans. 2) Effect of carbon sources on the lytic enzyme production by the K-42 strain was in the decreasing order of maltose>glucan>xylose>control in 2-day culture and of lactose>galactose>glucan>control in 3-day culture. Effect of inorganic nitrogen sources was in the decreasing order of ammonium acetate>sodium nitrate>control in 2-day culture and of ammonium chloride>ammonium oxalate>control in 3-day culture, whereas organic nitrogen sources except milk casein showed an increase in 2-day culture and a decrease in 3-day culture. Synergistic effect of carbon sources and nitrogen sources was not observed. 3) The enzyme production by the K-42 strain was greatly affected by pH change of the culture medium, thus a high lytic activity could be maintained by keeping the pH range of $7{\sim}8$ and adding carbon or nitrogen sources. 4) Optimum conditions for the lytic activity of the K-42 strain were obtained at $pH\;7{\sim}8$ and $60^{\circ}C$ and the extent of hydrolysis toward heated yeast cell wall was 65%.

• Journal of Microbiology and Biotechnology
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• v.28 no.11
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• pp.1946-1954
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• 2018

The aim of this study was to isolate and characterize a lytic Yersinia enterocolitica-specific phage (KFS-YE) as a biocontrol agent. KFS-YE was isolated and purified with the final concentration of ($11.72{\pm}0.03$) log PFU/ml from poultry. As observed by transmission electron microscopy, KFS-YE consisted of an icosahedral head and a contractile tail, and was classified in the Myoviridae family. KFS-YE showed excellent narrow specificity against Y. enterocolitica only. Its lytic activity was stable at wide ranges of pH (4-11) and temperature ($4-50^{\circ}C$). The latent period and burst size of KFS-YE were determined to be 45 min and 38 PFU/cell, respectively. KFS-YE showed relatively robust storage stability at -20, 4, and $22^{\circ}C$ for 40 weeks. KFS-YE demonstrated a bactericidal effect in vitro against Y. enterocolitica and provided excellent efficiency with a multiplicity of infection as low as 0.01. This study demonstrated the excellent specificity, stability, and efficacy of KFS-YE as a novel biocontrol agent. KFS-YE may be employed as a practical and promising biocontrol agent against Y. enterocolitica in food.

• Journal of Microbiology and Biotechnology
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• v.17 no.5
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• pp.745-752
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• 2007

A $\beta$-glucosidase from the algal lytic bacterium Sinorhizobium kostiense AFK-13, grown in complex media containing cellobiose, was purified to homogeneity by successive ammonium sulfate precipitation, and anion-exchange and gel-filtration chromatographies. The enzyme was shown to be a monomeric protein with an apparent molecular mass of 52 kDa and isoelectric point of approximately 5.4. It was optimally active at pH 6.0 and $40^{\circ}C$ and possessed a specific activity of 260.4 U/mg of protein against $4-nitrophenyl-\beta-D-glucopyranoside$(pNPG). A temperature-stability analysis demonstrated that the enzyme was unstable at $50^{\circ}C$ and above. The enzyme did not require divalent cations for activity, and its activity was significantly suppressed by $Hg^{+2}\;and\;Ag^+$, whereas sodium dodecyl sulfate(SDS) and Triton X-100 moderately inhibited the enzyme to under 70% of its initial activity. In an algal lytic activity analysis, the growth of cyanobacteria, such as Anabaena flos-aquae, A. cylindrica, A. macrospora, Oscillatoria sancta, and Microcystis aeruginosa, was strongly inhibited by a treatment of 20 ppm/disc or 30 ppm/disc concentration of the enzyme.

• Bulletin of the Korean Chemical Society
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• v.18 no.7
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• pp.761-766
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• 1997

Phospholipase C from Clostridium perfringens is known to catalyze the hydrolysis of phospholipids in biological membranes. In this study, a simple and sensitive method for assaying phospholipase C was developed by using liposomes entrapping calcein as a fluorescent marker. Phospholipase C-induced lysis of liposomes was determined by measuring the fluorescence intensity of calcein released out from liposomes, Various liposomes with different compositions were prepared by reverse-phase evaporation method to investigate the effect of liposomal composition on the lytic activity of phospholipase C. The calcein-entrapping efficiency of liposomes was affected by the chain length of fatty acid in phosphatidylcholine constituting liposomes. The lytic activity of phospholipase C was the highest against liposomes prepared with eggPC. The lytic activity decreased with increasing chain length of fatty acid in phosphatidylcholine. Incorporation of cholesterol more than 20% into the liposomal bilayer inhibited the phospholipase C-induced lysis. The lysis of liposomes was more greatly increased by the addition of 10 mM of calcium. The lytic activity of phospholipase C was also affected by the surface charge of liposomes. Taken together, it was concluded that reverse-phase evaporation vesicles composed of dipalmitoylphosphatidylcholine and cholesterol in the molar ratio of 9 : 1 allowed to detect the lowest concentration of phospholipase C (0.10 μg/assay volume). This study suggested that the use of liposomes can provide a simple, sensitive and inexpensive method for assaying phospholipase C.

• Food Science and Preservation
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• v.30 no.1
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• pp.42-51
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• 2023

This study aimed to characterize a lytic Salmonella Typhimurium-specific (ST) phage and its biofilm control capability against S. Typhimurium biofilm on polypropylene surface. ST phage was isolated, propagated, and purified from water used in a slaughterhouse. The morphology of ST phage was observed via transmission electron microscopy. Its bactericidal effect was evaluated by determining bacterial concentrations after the phage treatment at various multiplicities of infection (MOIs) of 0.01, 1.0, and 100. Once the biofilm was formed on the polypropylene tube after incubation at 37℃ for 48 h, the phage was treated and its antibiofilm capability was determined using crystal violet staining and plate count method. The phage was isolated and purified at a final concentration of ~11 log PFU/mL. It was identified as a myophage with an icosahedral head (~104 nm) and contractile tail (~90-115 nm). ST phage could significantly decrease S. Typhimurium population by ~2.8 log CFU/mL at an MOI of 100. After incubation for 48 h, biofilm formation on polypropylene surface was confirmed with a bacterial population of ~6.9 log CFU/cm². After 1 h treatment with ST phage, the bacterial population in the biofilm was reduced by 2.8 log CFU/cm². Therefore, these results suggest that lytic ST phage as a promising biofilm control agent for eradicating S. Typhimurium biofilm formed on food contact surfaces.

• Journal of Ginseng Research
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• v.13 no.2
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• pp.223-228
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• 1989

Natural killer (NK) cells are a heteroguneous subpopulation of lymphocytes that spontaneously exhibit cytotoxic activity against various virus-Infected and neoplastic target cells without prior exposure to a specific antigen. It was thought that NK calls play an important role in immunosurvrillanre against viral agents and tumors, and in prevention of metastasis. Recently, several reports have indicated evidence that ginseng extracts show a significant stimulatory effect on the humoral and cellular immune responses. This evidence gives support to the suggestion that the anticarcinogenic effect of ginseng may be due to the effect of ginseng on the immunological system. Treatment with total, diol, and triol saponin resulted in an increase in NK cytotoxic activity, but no enhancement of the lytic activity due to the natural killer cytotoxic factor (NKCF). Therefore, these results suggest that the augmentation of NK activity by ginseng saponin fractions may not be due to the activation of NKCF lytic activity.

• Korean Journal of Food Science and Technology
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• v.29 no.5
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• pp.1021-1027
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• 1997

We examined some properties of yeast cell wall lytic enzyme produced by Dicyma sp. YCH-37. Several metal ions, reducing reagents, and chemical modifiers have little effects on the lytic activity, except guanidine-HCl. Yeast cells of early log phase were more susceptible to the enzyme than those of stationary phase, and heat-treated cells were more easily lysed than intact living ones. Yeast cells pretreated with organic solvents such as butanol and acetone were more susceptible to the enzyme than intact living ones. Yeast cells cultured in Yeast extract-Malt extract medium containing 0.5 M ammonium sulfate were easily lysed by the lytic enzyme, and yeast cells cultured without shaking were more easily lysed by the enzyme than those with shaking. When SDS, ${\beta}-mercaptoethanol$, Triton X-100, sodium sulfite, and KCl were added to enzyme reaction mixture each, lysis of yeast cells was more effective.

• KSBB Journal
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• v.23 no.3
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• pp.187-192
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• 2008

Lysozyme-producing microorganisms were isolated to obtain bacteria which can efficiently solubilize microbial cells. Cells of normal and chloroform-treated Escherichia coli and Micrococcus Iysodeikticus were used as model substrates to isolate lysozyme-producing microorganisms and investigate the efficiency of cell lysis. The culture supernatant of the isolate New1 (98% similarity of 16S rDNA sequence with Thermomonas haemolytica) showed different lytic characteristics for different substrates. Thermal treatment (autoclave) of substrate cells showed a significant effect on cell solubilization by culture supernatant of the New1. For autoclaved substrate cells, E. coli, M. Iysodeikticus and chloroform-treated E. coli were solubilized by 58.7%, 49.4% and 79.1%, respectively, in the culture supernatant of New1. The lytic activity of New1 was mainly caused by lysozyme produced by the isolate. It was also showed that New1 exhibited high protease activity and a little cellulase activity.