Kussendrager K D, van Hooijdonk A C
DMV-International, R&D Center, Veghel, The Netherlands.
Br J Nutr. 2000 Nov;84 Suppl 1:S19-25. doi: 10.1017/s0007114500002208.
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.
乳过氧化物酶（LP）是牛乳中最显著的酶之一，它能催化乳过氧化物酶系统（LP-s）中多种微生物的失活。LP系统也被认为是人类分泌物（如唾液、泪液和乳汁）中的天然抗菌系统，并且被发现对哺乳动物细胞无害。LP的详细分子结构已被确定，LP-s产生的主要产物及其抗菌作用在很大程度上也已阐明。本文讨论了牛LP和LP-s的几个方面，包括物理化学性质、在牛奶和初乳中的存在情况以及作用机制。自从引入从牛奶和乳清中分离LP的工业工艺以来，人们对这种酶的兴趣大幅增加，并且将关注LP系统作为食品和其他产品生物防腐剂的潜在和实际应用。
