• Asian-Australasian Journal of Animal Sciences
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• v.15 no.6
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• pp.895-899
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• 2002

Lysozyme activity in buffalo milk in relation to the period of lactation, parity of animal, weather conditions and udder infections was studied. Effect of storage and heat processing of milk on lysozyme activity was determined. Lysozyme activity was higher in buffalo milk than in cow milk. Buffalo colostrum showed lysozyme activity 5 times of that in mature milk. Lysozyme activity in buffalo milk was not influenced by the parity of animal and the stage of lactation, however, it increased during extreme whether conditions (winter and summer). Lysozyme in both cow and buffalo milk exhibited maximum activity at pH 7.4. Buffalo milk lysozyme was fully stable while the cow milk lysozyme was partly inactivated by pasteurization (low temperature-long time as well as high temperature-short time treatments). Lysozyme in buffalo milk was more stable than in cow milk during storage and heat treatment. A 10 to 50-fold increase in milk lysozyme activity was observed in mastitic cows. An assay of lysozyme activity in milk can be used to diagnose mastitis in cattle but not in buffaloes. Some buffaloes exhibited 1000 fold greater lysozyme activity and moderately raised somatic cell count in milk, but there was no sign of mastitis in these animals. A possible role of milk lysozyme in prevention of mastitis in buffaloes is discussed.

• Journal of Applied Biological Chemistry
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• v.61 no.4
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• pp.367-370
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• 2018

Lysozyme is an antibacterial enzyme that is found in most of body fluids. Lysozyme in tears plays a primary role in protecting eye from harmful environments; if lysozyme is degraded or inhibited, eyes are likely to be more vulnerable to bacterial infection. In this study, lysozyme activity was evaluated according to varying concentrations of heavy metals, copper, zinc, cobalt and manganese and light metal, calcium that are frequently found in airborne particulate matters and was assayed using a dye-quenching lysozyme substrate, Micrococcus lysodeikticus. Less fluorescence intensity was observed with increasing amounts of copper, zinc, manganese and cobalt but not with calcium suggesting that these metals have some affinity with lysozyme and inhibit lysozyme activity. When albumin, the second most common protein in tears, was added on the reaction of lysozyme and metals, lysozyme activity was partially restored. This finding suggests that the albumin might protect damage caused by metals on lysozyme. To identify whether the decrease in enzymatic activity was related to structural changes of lysozyme, SDS-PAGE was conducted and only with copper did lysozyme show marked smearing bands on the SDS-gel, meaning that copper degraded lysozyme consistent with the sharpest activity decrease.

• Textile Coloration and Finishing
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• v.30 no.4
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• pp.264-274
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• 2018

Immobilization of lysozyme on chitosan non-woven using glutaraldehyde(GA) was investigated. For this, 100 % chitosan non-woven was prepared as novel support for the enzyme immobilization. In addition, free lysozyme activity was examined depending on various pH and temperature by measuring time. Moreover, the optimum immobilization conditions depending on various pH, temperature, immobilization time and lysozyme concentration was evaluated. In addition, thermal stability and storage stability of immobilized lysozyme were measured. The characteristics of immobilized lysozyme was examined by FT-IR, surface morphology, and MTT assay. The results are follows: the optimal immobilization of lysozyme were pH 7.0, $25^{\circ}C$, lysozyme concentration 1.5 mg/ml, immobilization time 240 min. The immobilized lysozyme showed higher thermal stability than the free trypsin. The immobilized lysozyme activity was retained 80 % of its initial activity at $4^{\circ}C$ over 30 days of storage. The lysozyme was immobilized effectively on chitosan non-woven by observation of surface morphology.

• The Korean Journal of Food And Nutrition
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• v.9 no.4
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• pp.447-451
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• 1996

Lytic activities of the egg white lysozyme from Korea-native Ogol fowl against the alkalophilic and thermophilic Bacillus sp. TA-11 were investigated and compared. Lytic activity of the Ogol fowl lysozyme for Bacillus sp. TA-11 was the highest for the cell of post-logarithm phase and optimum concentration of the lysozyme was 0.25%, Optimum reaction pH and temperature were 4.5 and 35$^{\circ}C$, respectively. Lytic activity of egg white lysozyme from fowl for Bacillus sp. TA-11 was the highest for the cell of stationary phase and optimum concentration of the lysozyme was 0.5%. Optimum reaction pH and temperature were 5.5 and 4$0^{\circ}C$, respectively.

• Journal of Microbiology and Biotechnology
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• v.24 no.10
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• pp.1405-1412
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• 2014

Lysozyme is a protein found in egg white, tears, saliva, and other secretions. As a marketable natural alternative to preservatives, lysozyme can act as a natural antibiotic. In this study, we have isolated Bacillus licheniformis TIB320 from soil, which contains a lysozyme gene with various features. We have cloned and expressed the lysozyme in E. coli. The antimicrobial activity of the lysozyme showed that it had a broad antimicrobial spectrum against several standard strains. The lysozyme could maintain efficient activities in a pH range between 3 and 9 and from $20^{\circ}C$ to $60^{\circ}C$, respectively. The lysozyme was resistant to pepsin and trypsin to some extent at $40^{\circ}C$. Production of the lysozyme was optimized by using various expression strategies in B. subtilis WB800. The lysozyme from B. licheniformis TIB320 will be promising as a food or feed additive.

• The Journal of Natural Sciences
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• v.14 no.2
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• pp.83-91
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• 2004

Recently phage K11 lysozyme was cloned and characterized in our lab. The K11 lysozyme was identified to have dual functions. It not only cuts a peptidoglycan bond in bacterial cell wall but also acts as an inhibitor of K11 RNA polymerase. It has been known that the T7 lysozyme binds specifically to T7 RNA polymerase and inhibits transcription. The dual activities of K11 lysozyme are atreeable to the case of T7 phage lysozyme and RNA polymerare. In order to identify the binding magnitude of K11 lysozyme with K11 RNA polymerase, yeast two-hybrid system was used. K11 phage lysozyme gene was introduced into pLexA plasmid and used as a prey. Also, K11 phage RNA polymerase gene was introduced into pJG4-5 and used as a bait. The binding between K11 lysozyme and K11 RNA polymerase was demonstrated by expression of reporter genes such as lacZ and leu2.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.21 no.4
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• pp.269-275
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• 1988

Inhibitory effects on bacterial growth by using lysozyme and mixtures of it with other antibacterial substances (sodium hexametaphosphate and sodium pyrophosphate) were investigated against the 7 kinds of hacterial strains isolated from putrefied surumi products. The growth inhibitory concentrations of lysozyme and lysozyme + sodium hexametaphosphate + sodium pyrophosphate against the bacteria were added to kamaboko, imitation crab meat and fried surumi, then viable cell count, pH and VBN were examined during the storage at $30^{\circ}C$ for 7 days. Lysozyme showed growth inhibitions against 6 of 7 isolates and the inhibition effect of mixture of antibacterial substances was multiplied against all the isolates compare with those of its individual use. Growth inhibitory effect of the substances on the bacteria was high in order of lysozyme + sodium pyrophosphate + sodium hexametaphosphate, lysozyme + sodium hexametaphosphate, lysozyme + sodium pyrophosphate and lysozyme. The most effective inhibitory concentration of mixture of the antibacterial substances in kamaboko and imitation crab meat was $0.05\%$ of lysozyme, $0.5\%$ of sodium pyrophosphate and $0.1\%$ sodium hexametaphosphate. But the bacterial growth was slightly inhibited in fried surumi even if the same concentration of the dipped mixture and the effect of the mixture was less than that of $0.2\%$ sorbic acid.

• Applied Chemistry for Engineering
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• v.9 no.6
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• pp.857-863
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• 1998

A simple and new experimental method for determination of lysozyme-M. lysodeikticus cell lysis reaction and lysozyme activity was suggested using Beer's law. The UV transmittance of the solution changed with the concentration of M. lysodeikticus and the relationship between the UV transmittance and M. lysodeikticus cell concentration followed Beer's Law. In addition, it was experimentally proven that the UV transmittance of the solution was not influenced by the lysozyme concentration and product of the lysis reaction. During the lysozyme-M. lysodeikticus cell lysis reaction, thus, M. lysodeikticus cell concentration in the solution could be measured in-situ by UV-spectrophotometer. By using these experimental data, kinetic Parameters of the Michaelis-Menten equation for the lysozyme-M. lysodeikticus cell 1ysis reaction was simply determined The maximum reaction rate constant ($k_3$) and Michaelis-Menten constants were $0.1734sec^{-1}$ and $9.83{\times}10^{-6}M$ respectively. The activity of the lysozyme could also be obtained with this experiment because the lysis reaction rate of the 1ysozyme depended on its activity.

• Journal of Korean Ophthalmic Optics Society
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• v.2 no.1
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• pp.85-90
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• 1997

The cornea and conjunctiva of the human eye are exposed to external environment and thus are damageable. If the damaged part is infected with some pathogenic microorganisms. serious visual loss may be occured by inflammation. Keratitis or conjunctivitis does not always occur if the eyes are routinely exposed to pathogenic factors because lysozyme in human tears has antimicrobial activity against the microorganisms. 10 this study we have selected 5 strains causing keratitis and/or conjunctivitis. and cultured them in the optimum media. And then we have estimated the growth inhibition of the strains with the addition of various concentration of lysozyme to media to investigate the antimicrobial activity of lysozyme. The results are as follows. The growth of the strains were decreased according to the increase of lysozyme concentration. The growth of Pseudomonas. Neisseria. Klebsiella and Staphylococcus were inhibited 43%, 41%, 35% and 22% respectively by 1 mM concentration of lysozyme. The susceptibility of the gram-negative bacteria to lysozyme is 1.5~2 times higher than the Staphylococcus which is gram-positive bacteria in 1 mM concentration of lysozyme. But lysozyme inhibited the growth of Fusarium which is fungi slightly.

• Korean Journal of Food Science and Technology
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• v.24 no.1
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• pp.11-13
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• 1992

Effect of 200 ppm lysozyme. 0.1 glycine and 0.1% lysine on inhibition growth of Lactobacillus plantarum was investigated in MRS broth. All samples except control were effective in inhibiting the growth and especially the combination of lysozyme and glycine was observed to be highly effective. The mixture effect against microbial growth was increased as concentration of lysozyme with glycine or lysozyme with EDTA was respectively increased. Lactobacillus plantarum almost didn't grow in MRS broth containing lysozyme(>200 ppm) with glycine(>0.5%), or lysozyme(>200 ppm) with EDTA(> 0.8 mM). It was found that the growth of L. plantarum could be extremely inhibited in 120 ppm lysozyme with at least 0.8 mM EDTA compared with control.