• The Journal of Natural Sciences
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• v.7
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• pp.53-58
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• 1995

To elucidate the effect of egg white lysozyme from Ogol fowl on the preservation of milks, fishcurd and sausage, changes of pH, volatile base nitrogen content and viable cell count were investigated during the storage periods at $20^{\circ}C$, $30^{\circ}C$ and $37^{\circ}C$ after the addition of lysozyme in each foods. Volatile base nitrogen count of raw milk as marker of spoilage was lowest(63 mg%) in 0.05% lysozyme addition lot which was stored at $20^{\circ}C$ for 2 days, and its preservation effect by lysozyme at $30^{\circ}C$ was enhanced with addition of glycine(0.1%). Preservation effect by lysozyme in commercial milk at $37^{\circ}C$ and in fishcurd at $5^{\circ}C$ and $20^{\circ}C$ were also good, and when sausage was stored at $5^{\circ}C$ after treatment of lysozyme instead of sorbic acid, its preservation effect was acceptable.

• 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.

• Animal cells and systems
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• v.13 no.3
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• pp.345-350
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• 2009

We have isolated and characterized a new insect chicken type (c-type) lysozyme gene from the common cutworm, Spodoptera litura. The full-length cDNA of Spodoptera lysozyme is cloned by rapid amplification of cDNA ends PCR (RACE-PCR). The isolated cDNA consists of 1039 bp including the coding region for a 142-amino acid residue polypeptide, which included a signal peptide of 21-amino acid residue and a mature protein of 121-amino acid residue. The predicted molecular weight of mature lysozyme and its theoretical isoelectric point from amino acid composition is 13964.8 Da and 9.05, respectively. The deduced amino acid sequence of Spodoptera lysozyme gene shows the highest similarity (96.7%) to Spodoptera exigua lysozyme among other lepidopteran species. Amino acid sequence comparison with other the c-type lysozymes, Spodoptera lysozyme has the completely conserved $Glu^{32}$ and $Asp^{50}$ of the active site and eight Cys residues are completely conserved in the same position as that of other lepidopteran lysozymes.

• Korean Journal of Poultry Science
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• v.16 no.3
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• pp.157-167
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• 1989

Pretreatment of egg white and ion exchange resins was attempted to separate lysozyme from egg white efficiently. Apparent viscosity of egg white could be decreased to 3cp by homogenization for 30 minutes at 2, 000rpm and ultrasonication for 45 minutes. The result of testing adsorption capacity of lysozyme was as follows； CM-Sephadex C-25 ＞Duolite C464＞Amberlite C-50＞Dowex MSC-1＞Amberlite IRC-50＞Amberlite IRC-84. Although CM-Sephadex C-25 showed highest adsorption capacity of lysozyme, egg white could not eluted easily. Duolite Cf64 was selected based on relatively high lysozyme adsorption and good egg white eluting property for separation of egg white lysozyme. Na$^{＋}$ form of Duolite C-464 was most effective on adsorption of Iysozyme. To separate lysozyme from egg white efficiently rinse buffer and eluting solution were selected 0.1M sodium phosphate buffer at pH 6.5 and 10% ammonium sulfate respectively. After separating lysozyme from egg white, foaming power of egg white was decreased to 85.3%. Color of egg white gel was not changed while hardness of egg white gel was decreased by 30% after separating lysozyme. However, elasticity of egg white gel was increased by 13% in lysozyme-separated egg white.

• 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.

• Korean Journal of Poultry Science
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• v.17 no.2
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• pp.109-114
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• 1990

Enzymatic activity of isolated Lysozyme from egg white by cation ion-exchange chromatography was detected with various methods and stability of lysozyme in solution was studied by heat and pH treatments. Lysozyme activity refered to mg pure lysozyme/mg sample was more accurate although it needed standard lysozyme. But lysozyme activity refered to units/mg sample could be detected easily and reducted total detection time. Enzymatic activity of isolated lysozyme which dissolved in 0.066M phosphate buffer(pH 6.3) and then incubated at $37^{\circ}C$ for 2hr was increased remarkably on the lysis of Micrococcus lysodeikticus. The activity of isolated lysozyme by CM Sephadex C-25 was higher in eluting solution of above O. D. 1.0 at 640nm and attained 36, 000 units/mg solid. The stability of isolated lysozyme was decreased by various heat treatment. Activity began to decrease above 6$0^{\circ}C$ and dropped rapidly at $100^{\circ}C$. Especially, 35% loss of activity occured in 0.066M phosphate buffer at $100^{\circ}C$. for 15min. The stability of lysozyme was also affected by pH. lysozyme was very stable in acidic solution but in alkaline solution. Enzymatic activity showed maximum value at pH 3.0 solution while decreased rapidly above pH 6.0 solution.

• 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.

• Applied Biological Chemistry
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• v.33 no.3
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• pp.252-256
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• 1990

Characteristics of brewing product, Mageoly mashes diluted by the same ratio of water was investigated for alcohol formation, pH change, acid formation nucleotide content and sensory evaluation stored at $3^{\circ}C\;or\;30^{\circ}C$ during 7 days. Each sample was mixed with lysozyme 270ppm and glycine 0.27%, or lysozyme 450ppm and glycine 0.45% on the secondary brewing process in Mageoly brewing. The brewing was not affected by addition of lysozyme and glycine mixture. When the lysozyme-glycine mixture was added during brewing, that resulted in a decrease in pH, a suppression of acid formation and an increase in IMP and inosine content Therefore ere was significantly improved in taste and palatability.

• Animal cells and systems
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• v.12 no.3
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• pp.149-155
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• 2008

We have isolated and characterized Agrius convolvuli cDNA encoding a c-type lysozyme. The cDNA sequence encodes a processed protein of 139 amino acid residues with 19 amino acid residues amino-terminal signal sequence and 120 amino acid residues mature sequence. The amino acid residues responsible for the catalytic activity and the binding of the substrate are conserved. Agrius lysozyme has a high identity to Manduca sexta. Recombinant A. convolvuli lysozyme was expressed in Escherichia coli BL21(DE3) pLysS cells for pGEX 4T-1 expression vector. Their optimal conditions for the fusion protein expression and purification were screened. Lysozyme gene amplified with primers ACLyz BamHI and ACLyz XhoI was ligated into the pGEX 4T-1 vector, which contained the glutathione S-transferase(GST) gene for fusion partner. The fusion protein was induced by IPTG and identified by SDS-PAGE analysis. Molecular weight of the fusion protein was estimated to be about 45 kDa. Recombinant lysozyme, fused to GST, was purified by glutathion-Sepharose 4B affinity chromatography. Western blot analysis of this protein revealed an immunoreactivity with the anti-Agrius lysozyme.

• Asian-Australasian Journal of Animal Sciences
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• v.14 no.4
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• pp.462-466
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• 2001

To understand molecular mechanisms of mouse mammary gland involution, clones were isolated by differential screening of a cDNA library. Partial sequences of a clone showed 100% identity to cDNA sequences of mouse lysozyme P gene. Northern analysis was performed to examine expression levels of lysozyme mRNA in mammary gland at several physiological states. Expression of lysozyme gene was induced at involution day 5 compared with lactating stage. High levels of lysozyme mRNA were also detected at virgin tissues. Two types of separate genes, P and M lysozyme, have been known in mouse, and we found that both lysozyme P and M genes were expressed in mammary tissues by reverse transcriptase-polymerase chain reaction. The lysozyme enzyme activity determined by lysoplate assay was also higher in involuted mammary tissues compared with lactating tissues, showing a similar trend to its mRNA levels. Lysozyme is an antimicrobial protein and involved in host defense mechanism. The increase in lysozyme gene expression may help to prevent microbial infection during mammary gland involution at which stage the residual milk in the mammary gland provides good nutritional sources for microbial growth.