Lactoperoxidase:
physico-chemical properties, occurrence, mechanism of action and applications.
Kussendrager
KD, van Hooijdonk AC.
DMV-International,
R&D Center, Veghel, The Netherlands. kussendr@dmv-international.com
Lactoperoxidase
(LP) is one of the most prominent enzymes in bovine milk and catalyses
the inactivation of a wide range of micro-organisms in the lactoperoxidase
system (LP-s). LP-systems are also identified as natural antimicrobial
systems in human secretions such as saliva, tear-fluid and milk and
are found to be harmless to mammalian cells.
The detailed
molecular structure of LP is identified and the major products generated
by the LP-s and their antimicrobial action have been elucidated for
the greater part.
In this paper
several aspects of bovine LP and LP-s are discussed, including physico-chemical
properties, occurrence in milk and colostrum and mechanisms of action.
Since the introduction of industrial processes for the isolation of
LP from milk and whey the interest in this enzyme has increased considerably
and attention will be paid to potential and actual applications of
LP-systems as biopreservatives in food and other products.
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