Lactoferrin is an iron-binding protein from the transferrin family and was first isolated from milk. Lactoferrin is produced by polymorph nuclear leukocytes and epithelial cells of many mammalian species and is present in such mucosal secretions as tears, saliva, seminal and vaginal fluids as well as in several organs and blood. Many biological functions of lactoferrin have been identified: iron absorption, bacteriostatic, bactericidal, fungicidal, antiviral, antiparasitic and antitumour activities. It is also well known for its immunomodulatory and antiinflammatory properties. Additionally, lactoferrin is thought to possess protease, ribonuclease, procoagulant and transcription factor activities. Nowadays bovine lactoferrin is isolated and purified on an industrial scale and used for food preservation and production of infant formulas, yogurt, skim milk, chewing gum, cosmetic formulas, nutritional supplements and therapeutic supplements for pets. The use of lactoferrin as an immunostimulator is a promising area especially in the case of patients with immunosupression.
The quality of silages made from raw potatoes preserved preliminary with sulphuric, hydrochloric, phosphoric and formic acid and with the Acidol preparation was compared with that of silages made in acid whey. The period of ensiling whole tubers in whey pickle is approximately fourfold longer than that of ensiling tubers without peel and/or cut tubers. Tubers cut into pieces are ensiling as quickly as suedes, beets, pumpkin or cabbage. In the whey pickle tubers damaged during harvest and tubers infested by dry rot can be ensiled. This ensiling way is not suitable for tubers heavily infected by soft rot. Silages made from raw potatoes preserved with acids have got the estimates from bad to statisfactory. The quality of silages made in whey pickle was good or very good. Potatoes ensiled in whey contain a very low amount of butyric acid and are willingly eaten by pigs.
By now, over 800 different antimicrobial peptides have been identified in fauna and flora. Antimicrobial peptides (AMPs) are an important part of the innate immunity of all living organisms. The first animal AMP was found in 1962 by Kiss and Michl in the venomous skin secretion of the orange speckled frog Bombina variegata. Most known AMPs are multifunctional as effectors of innate immunity and have direct antimicrobial activity against various bacteria, enveloped viruses, and fungi. Most of them share a common mechanism of antimicrobial action: permeabilization of the cell membrane of the pathogen. There is a real chance to use these peptides for developing a new generation of medicines. The present review outlines the history of studies on antimicrobial peptides and the current state of knowledge about their activity.