Refined hemisphaericin stabilization by microencapsulation with arabic gum and spray drying

Abstract

Hemisphaericin, the protease from the fruits of Bromelia hemisphaerica, is found as a complex of nine multiple molecular forms, identified by isoelectric points distributed over a pH range from 3.5 to 9.0 (Garduño et al. 1974). Cortés-Vázquez et al. (2008) have reported the purification and characterization of hemisphaericin-C, a 24 kDa cationic protease with primary substrate specificity of dual type. On the other hand, several studies on industrial applications for hemisphaericin have been carried out successfully, including fish protein solubilization, beer chill proofing, malt adjunct hydrolysis, plant protein functional property improvement (Briones-Martínez et al. 1994), and antioxidative peptide production from whey proteins (Palma-Rodríguez 2008).