SCIENTIFIC DATA & DIAGNOSTIC SERVICES

Click LYSOZYME MIC DATA to see a list of bacteria sensitive to Lysozyme Click LYSOZYME HYDROCHLORIDE FOOD GRADE to see Specifications

Model studies show Lysozyme has antibacterial activity against many pathogenic organisms, (under certain conditions, alone or combined with other potentiating compounds), including: Clostridia tyrobutyricum, Clostridia botulinum, Campylobacter jejuni, Listeria monocytogenes, Pseudomonas spp., Salmonella enteretidis, Clostridium thermosaccharolyticum and Bacillus stearothermophilus.

Lysozyme activity is demonstrated to be effective by attacking the cell wall polysaccharide of different bacterial species, which leads to a break down of the cell wall and destruction of the micro-organisms. Lysozyme is most effective in hydrolyzing a tetrasaccharide found usually in Gram-positive bacteria. Lysozyme can withstand a temperature of 55 – 56 °C. for about one hour (such as in the standard “cooking process” of the curd in production of hard cheese like Grana).  Generally, lysozyme can withstand a temperature up to 70 °C to 80 °C.  for just a couple of minutes at an acidic pH. It is advisable to add lysozyme to the milk after pasteurization in order to avoid any inactivation of the enzyme during a heating process.

A short video about the structure and action of Lysozyme

Egg white consists of 88-89% water and 11-12% protein, namely 54% Ovalbumin, 12% Ovotransferrin, 11% Ovomucoid, 8% Globulins, 3.5% Ovomucid, 3.4% Lysozyme and 0.05% Avidin.  Extracted from hen egg whites, the natural polypeptide Lysozyme contains 129 amino acid residues (21 Aspartic acid, 5 Glutamic acid, 12 Alanine, 11 Arginine, 8 Cysteine, 3 Phenylalanine, 12 Glycine, 6 Isoleucine, 1 Histidine, 8 Leucine, 6 Lysine, 2 Proline, 2 Methionine, 10 Serine, 3 Tyrosine, 7 Threonine, 6 Tryptophan and 6 Valine).  Its structure contains 4 disulphide bridges. The molecular weight is about 14,400 Dalton. The preponderance of basic amino acid residues confers a basic character to the natural Lysozyme molecule; its isolectric point is 10.5-11.0.

LYSOLAC Trial / Vermont 04.14.07

• Type of Cheese: Gouda
• Lysozyme Dosage: 35g/1000L : 75g/4000L
• Spore Concentration: 480 MPN/L

The following data, from a trial with Gouda cheese, demonstrates the immediate effectiveness of
LYSOLAC against Clostridia tyrobutyricum spores. (Notice how it binds immediately to the casein and remains in the curd)

Results
The analysis of curd, whey and cheese confirm effective treatment. Notice how the Lysozyme, once added to the milk, immediately binds to the casein and remains in the curd, leaving hardly a trace in the whey; after 9 weeks the cheese shows the remaining presence of LYSOLAC, which then continues to protect against late blowing for years.

	Raw Milk	Whey	Curd	Cheese
Spores MPN/L or gr	480	0	2	1.8
LYSOLAC µg/ml or mg	52	2.2	270	292

DIAGNOSTIC SERVICES

As Clostridia tyrobutyricum spores can vary in amount greatly throughout the year, depending on various conditions such as climate and types of feed, the safest approach is to dose at 30mg year round. You cannot over dose. For a precise prescription, we recommend you get your milk tested (click here for more information). Our own laboratories together with other collaborative partnerships can provide analysis, support and all necessary resources for our customers.  Click here to calculate your particular dosage.

THE GC TEST
bioseutica now provides the cheese industry with a powerfully accurate analytical service to determine the exact cause of blowing defects during aging.  This innovative technique uses Gas Chromatography to extract volatile fatty acid profiles from your cheese samples, thus clarifying whether the blowing defects are due to butyric, proprionic, coliform or hetero-fermentative bacteria. For details call toll-free 1-877-785-8421 or click here.

Toxicology and Safety Statement
Lysozyme is a naturally occurring protein discovered by Fleming in 1922. Hen egg-white (HEW) Lysozyme, known as one of the most powerful natural antibacterial and antiviral compounds, has been used in foods and pharmaceutical compositions since the 1950's. Numerous toxicological studies over the years, including acute, sub-acute and chronic toxicity studies on animals, have demonstrated that HEW Lysozyme is "devoid of toxic effects even after rather prolonged administration". Moreover, on the basis of toxicological data obtained in numerous clinical studies by 20-40 day treatments in doses of 1.5 g or more by the oral or parenteral route, "no particular problems of local and systemic tolerance of Lysozyme have become apparent".

The overall results of studies on major vital functions, such as the cardiovascular system, the automatic nervous system and the thermoregulatory system confirm the non toxicity of HEW Lysozyme.

Lysozyme has been affirmed as GRAS by the FDA with its tentative final rule dated March 13, 1998.
The USDA authorized the use HEW Lysozyme as an ingredient in or on processed products labeled as "Organic".

The JEFCA-Joint FAO/WHO Expert Committee on Food Additives stated in its report that: "Lysozyme is obtained from edible animal tissue commonly used as food and can thus be designed as class I enzyme and regarded as a food. It was therefore considered acceptable for use in food processing when used in accordance with good manufacturing practice".

HEW Lysozyme is an egg protein. Therefore, individuals sensitive to egg Lysozyme may experience an allergic reaction if taking HEW Lysozyme systemically (i.e. intra-venous, inhalation, etc.). However, of all the egg-white proteins, Lysozyme has the least statistical allergenic incidence. Consider this: allergies to proteins of animal origin such as milk, egg and cod are present in less than 0.3% of the population. While infants and small children are the most sensitive to eggs (31%), 8% of adults with food allergies are allergic to eggs. Of all egg allergic individuals, 35% have shown to have anti-Lysozyme IgE, or an incidence of 0.0084% of the population.  

In fact, the statistical incidence of spontaneous or acquired hypersensitivity episodes to Lysozyme as a pharmaceutical, is - according to some published reports - extremely low (less than 1:1,000,000 doses) and “much lower than that of other commonly used drugs which also have a protein structure, such as insulin, ACTH and other".

In a recent study related to processing aids in wine making, carried out in Germany and France over a 3 year period, only 8 egg-allergic individuals could be recruited out of at least 3,000 food allergic patients screened a year. This prompted the researchers to state that "if it is such a problem to find this type of allergy among adults, it poses the question about the scope of the actual problem in the European population".   Another recent study, published by the The American College of Nutrition,  found that “the use of Lysozyme as an additive in Grana Padano does not appear to be harmful in egg allergic subject.”  To see the study click here.

Not withstanding the above, bioseutica is extremely receptive to the allergenicity issues and is supportive of the regulatory bureaus' initiatives regarding allergen labeling in food, provided that the reasons for such initiatives are supported, in the interest of objective scientific decision making, by reliable scientific data, such as double blind placebo control tests, and not just by anecdotal observations.

Indeed, bioseutica believes that the benefits of HEW Lysozyme are such that labeling its presence in pharmaceutical compositions and foodstuff should not be seen as merely a mean to inform the concerned consumer, but, also, as a marketing tool for the manufacturer. In fact, to publicize a food product as "containing" or "fortified" with Lysozyme communicates to the consumer that such product is, or has been preserved, processed, and protected with a natural and safe compound, which, in certain instances, is also known to improve the flavor, color and texture of such food.

http://www.ams.usda.gov/nop/Newsroom/FedReg09_11_06TM-04-01.pdf
http://www.inchem.org/documents/jecfa/jecmono/v30je04.htm

Fleming's Lysozyme Luigi Barbara and Rinaldo Pellegrini. Edizioni Minerva Medica, 1976 pp.53
Fleming's Lysozyme Luigi Barbara and Rinaldo Pellegrini. Edizioni Minerva Medica, 1976 pp.123
Ricerche farmacologiche sul lisozima Gialdroni Grassi G. Terapia antibiottici Chemoterapie, 6, 89, 1956
Direct Food Substances Affirmed As Generally Recognized As Safe Food & Drug Administration. Federal Register, Vol. 63 No.49. March 13, 1998. 21 CFR Part 184 [docket no. 89G-0393]
Update on Food Allergy. Sampson HA. J. Allergy Clin. Immunol 2004; 113:805.-19
Prevalence of Lysozyme sensitization in an egg-allergic population. Fremont S. et al Allergy. 1997 Feb;52(2):224-8
Fleming's Lysozyme Luigi Barbara and Rinaldo Pellegrini. Edizioni Minerva Medica, 1976 pp.124
Allergenicity study of protein concerning processing aids for wine 2006 Aug; part 7 Conclusion
"Department of Dermatology and Allergy Biederstein" Allergenicity study of protein concerning processing aids for wine 2006 Aug; 6.3.1.pp 83
Allergenicity study of protein concerning processing aids for wine 2006 Aug; part 7, 88

LYSOLAC Granular

LYSOLAC Solution