Lactoperoxidase partitioning from whey using the reverse micelles of non‐ionic/ionic mixed surfactants: Improvement of back extraction

Abstract

Biopreservatives are gaining the importance in the food industry as an alternative to the harmful chemical preservatives. Though few natural antimicrobials are available from microbial sources, their growth and the related upstream are additional steps for industry.Industries are constantly seeking cheap sources of biopreservatives.Of the many identified biopreservatives, Lactoperoxidase (LP -EC 1.11.1.7) is popular and proven to be effective. As a part of the natural defense system in mammals, it is a component of the secretory glands. LP is a calcium-containing glycoprotein with 8%-10% carbohydrate. The enzyme consists of 612 amino-acids and heme on a single polypeptide chain with an approximately 78 kDa molecular weight and an isoelectric point between 9.2 and 9.9 (Kussendrager & van Hooijdonk, 2000). The maximum optical absorbance of LP was 412 nm. The enzyme is highly heat-stable under pasteurization conditions and also relatively stable against proteolytic enzymes. Whey, the by-product of cheese manufacturing, is a cheap source of LP.Bovine LP alone is inactive against microbes; however, the reaction products catalyzed by LP are harmful to the infecting microbes yet are safe for humans. The antimicrobial property of Lactoperoxidase is increasingly explored in the food and pharma industry. Apart from its antimicrobial nature, LP also exhibits antioxidant and anticancer properties (Abu-Serie & El-Fakharan, 2017;Albera & Kankofer, 2009).Whey contains considerable amounts of LP along with other major proteins that include beta-lactoglobulin, alpha-lactalbumin, bovine serum albumin (BSA), Lactoferrin (Lf), and glycomacropeptide. The extraction and purification of LP are difficult as the other major and minor whey proteins hinder the purification process,