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Lysozyme from chicken egg white Sale

(Synonyms: 鸡蛋清溶菌酶) 目录号 : GC33922

Lysozymefromchickeneggwhite是鸡蛋中存在的一种溶菌酶,可分解革兰氏阳性菌。

Lysozyme from chicken egg white Chemical Structure

Cas No.:12650-88-3

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1g
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实验参考方法

Kinase experiment:

For measurement of lytic activity in egg white at each pH, temperature, and CO2 condition, eggs are randomly selected from a flat of eggs (2 dozen eggs) obtained from a local grocery store. To determine the amount of egg white to be added to obtain a 0.001% lysozyme concentration, it is documented that chicken egg white contains approximately 3.4% lysozyme. For determining egg white activity, 0.030 g of albumen was added to 100 mL of the buffered solutions. This equated to a concentration of approximately 0.001% lysozyme. In addition, the egg white contains other antimicrobial proteins that are naturally present, as mentioned in the Introduction section[1].

References:

[1]. Banerjee P, et al. Influence of carbon dioxide on the activity of chicken egg white lysozyme. Poult Sci. 2011 Apr;90(4):889-95.

产品描述

Lysozyme from chicken egg white is a bactericidal enzyme present in chicken eggs, and it lyses gram-positive bacteria.IC50 & Target: Bacteria[1]In Vitro: Lysozyme is an ubiquitous enzyme. The hen egg is the most abundant source of lysozyme, which constitutes approximately 3.4% of the albumen proteins. Lysozyme is a natural antimicrobial that hydrolyzes the β(1-4) glycosidic linkage between N-acetylmuramic acid and N-acetylglucosamine found in the peptidoglycan layer of the bacterial cell wall and causing cell lysis. The bactericidal effect of lysozyme is primarily limited to gram-positive bacteria, including pathogens such as Listeria monocytogenes and certain Clostridium species as well as some spoilage organisms, including thermophilic spore-forming bacteria and certain yeasts. The gram-negative bacteria are more resistant to lysozyme action because of their complex cell wall structure[1].

Lysozyme is an ubiquitous enzyme. The hen egg is the most abundant source of lysozyme, which constitutes approximately 3.4% of the albumen proteins. Lysozyme is a natural antimicrobial that hydrolyzes the β(1-4) glycosidic linkage between N-acetylmuramic acid and N-acetylglucosamine found in the peptidoglycan layer of the bacterial cell wall and causing cell lysis. The bactericidal effect of lysozyme is primarily limited to gram-positive bacteria, including pathogens such as Listeria monocytogenes and certain Clostridium species as well as some spoilage organisms, including thermophilic spore-forming bacteria and certain yeasts. The gram-negative bacteria are more resistant to lysozyme action because of their complex cell wall structure[1].

[1]. Banerjee P, et al. Influence of carbon dioxide on the activity of chicken egg white lysozyme. Poult Sci. 2011 Apr;90(4):889-95.

Chemical Properties

Cas No. 12650-88-3 SDF
别名 鸡蛋清溶菌酶
分子式 分子量
溶解度 Water : 10 mg/mL 储存条件 -20°C, protect from light
General tips 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液;一旦配成溶液,请分装保存,避免反复冻融造成的产品失效。
储备液的保存方式和期限:-80°C 储存时,请在 6 个月内使用,-20°C 储存时,请在 1 个月内使用。
为了提高溶解度,请将管子加热至37℃,然后在超声波浴中震荡一段时间。
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动物体内配方计算器 (澄清溶液)

第一步:请输入基本实验信息(考虑到实验过程中的损耗,建议多配一只动物的药量)
给药剂量 mg/kg 动物平均体重 g 每只动物给药体积 ul 动物数量
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Research Update

Purification of Lysozyme from chicken egg white using diatom frustules

Food Chem 2019 Jul 15;286:483-490.PMID:30827636DOI:10.1016/j.foodchem.2019.02.023.

A nontoxic chromatographic matrix, with low cost and high adsorption capacity, is always a major goal for therapeutic protein purification. In this study, the frustules from two cultured diatoms, Nitzschia bilobata (AQ1) and Psammodictyon panduriforme (NP), were investigated as cation exchange materials for lysozyme purification from chicken egg white. The surface area and cation exchange capacity of frustules were about 400 m2/g and 140 μmol/mL for AQ1, 390 m2/g and 130 µmol/mL for NP. The optimal pH was 9 for adsorption. Through batch purification, the lysozyme recovery was 86% with a purity of 95% by AQ1 frustules, which was higher than that by NP frustules (82% with a purity of 90%). In the flow-through system, the purity using AQ1 frustules notably increased to 99%, higher than the result of 91% using NP frustules. Diatom frustules from AQ1 are more effective and could be an alternative chromatographic matrix for lysozyme purification.

Purification of Lysozyme from chicken egg white by high-density cation exchange adsorbents in stirred fluidized bed adsorption system

Food Chem 2021 May 1;343:128543.PMID:33187742DOI:10.1016/j.foodchem.2020.128543.

Lysozyme from crude chicken egg white (CEW) feedstock was successfully purified using a stirred fluidized bed adsorption system ion exchange chromatography where STREAMLINE SP and SP-XL high density adsorbents were selected as the adsorption carrier. The thermodynamic and kinetic studies were carried out to understand the characteristics of lysozyme adsorption by adsorbents under various conditions, including adsorption pH, temperature, lysozyme concentration and salt concentrations. Results showed that SP and SP-XL adsorbents achieved optimum lysozyme adsorption at pH 9 with capacity of ~139.77 and ~251.26 mg/mL, respectively. The optimal conditions obtained from batch studies were directly employed to operate in SFBA process. For SP-XL adsorbent, the recovery yield and purification factor of lysozyme were 93.78% and ~40 folds, respectively. For SP adsorbent, lysozyme can be eluted ~100% with purification factor of ~26 folds. These two adsorbents are highly suitable for use in direct recovery of lysozyme from crude CEW.

Effective purification of Lysozyme from chicken egg white by tris(hydroxymethyl)aminomethane affinity nanofiber membrane

Food Chem 2020 Oct 15;327:127038.PMID:32447136DOI:10.1016/j.foodchem.2020.127038.

Polyacrylonitrile nanofiber membrane functionalized with tris(hydroxymethyl)aminomethane (P-Tris) was used in affinity membrane chromatography for lysozyme adsorption. The effects of pH and protein concentration on lysozyme adsorption were investigated. Based on Langmuir model, the adsorption capacity of P-Tris nanofiber membrane was estimated to be 345.83 mg/g. For the operation of dynamic membrane chromatography with three-layer P-Tris nanofiber membranes, the optimal operating conditions were at pH 9, 1.0 mL/min of feed flow rate, and 2 mg/mL of feed concentration. Chicken egg white (CEW) was applied as the crude feedstock of lysozyme in the optimized dynamic membrane chromatography. The percent recovery and purification factor of lysozyme obtained from the chromatography were 93.28% and 103.98 folds, respectively. Our findings demonstrated the effectiveness of P-Tris affinity nanofiber membrane for the recovery of lysozyme from complex CEW solution.

Purification of Lysozyme from chicken egg white using nanofiber membrane immobilized with Reactive Orange 4 dye

Int J Biol Macromol 2019 Aug 1;134:458-468.PMID:31078593DOI:10.1016/j.ijbiomac.2019.05.054.

Nanofiber membrane chromatography integrates liquid membrane chromatography and nanofiber filtration into a single-step purification process. Nanofiber membrane can be functionalised with affinity ligands for promoting binding specificity of membrane. Dye molecules are a good affinity ligand for nanofiber membrane due to their low cost and high binding affinity. In this study, a dye-affinity nanofiber membrane (P-Chitosan-Dye membrane) was prepared by using polyacrylonitrile nanofiber membrane modified with chitosan molecules and immobilized with dye molecules. Reactive Orange 4, commercially known as Procion Orange MX2R, was found to be the best dye ligand for membrane chromatography. The binding capacity of P-Chitosan-Dye membrane for lysozyme was investigated under different operating conditions in batch mode. Furthermore, desorption of lysozyme using the P-Chitosan-Dye membrane was evaluated systematically. The recovery percentage of lysozyme was found to be ~100%. The optimal conditions obtained from batch-mode study were adopted to develop a purification process to separate Lysozyme from chicken egg white. The process was operated continuously using the membrane chromatography and the characteristic of the breakthrough curve was evaluated. At a lower flow rate (i.e., 0.1 mL/min), the total recovery of lysozyme and purification factor of lysozyme were 98.59% and 56.89 folds, respectively.

Strong and weak cation-exchange groups generated cryogels films for adsorption and purification of Lysozyme from chicken egg white

Food Chem 2021 Apr 16;342:128295.PMID:33092916DOI:10.1016/j.foodchem.2020.128295.

Here, the macroporous poly(hydroxylmethyl methacrylate/glycidyl methacrylate [p(HEMA-GMA)] cryogels with large porous surface were prepared, and then the epoxy groups of the p(HEMA-GMA) cryogels were systematically modified into strong and weak cationic groups. The effects of initial protein concentrations, adsorption time, pH, salt concentrations and temperatures on adsorption efficiency of cation exchange cryogels for lysozyme were determined. The maximum lysozyme adsorption capacities of strong and weak cation exchange cryogels were found to be 188.3 and 79.7 mg/g cryogel at 25 °C, respectively. The performance of the strong cationic cryogel was evaluated by purification of lysozyme from egg white. The activity of the isolated lysozyme was found to be 21,347 U/mg. The cationic cryogel maintained its expected high adsorption capacity and efficiency of the purification levels during repeated adsorption desorption processes. Finally, the purpose of this work is the design a cation exchange system for purification of lysozyme from egg-white.