title: Prolyl-specific peptidases for applications in food protein hydrolysis.
abstract: Various food proteins including, e.g. gluten, collagen and casein are rich in L-proline residues. Due to the cyclic structure of proline, these proteins are well protected from enzymatic degradation by typical digestive enzymes. Proline-specific peptidases (PsP) belong to different families of hydrolases acting on peptide bonds (EC 3.4.x.x). They occur in various organisms including bacteria, fungi, plants and insects. Based on their biochemical characteristics, PsP type enzymes are further grouped into different subclasses of which prolyl aminopeptidases (EC 3.4.11.5, PAP), prolyl carboxypeptidases (EC 3.4.17.16, PCP) and prolyl oligopeptidases/prolyl endopeptidases (EC 3.4.21.26, POP/PEP) are of major interest for applications in food biotechnology. This mini review summarises the biochemical assays employed for these subclasses of PsP and their structural properties and the reaction mechanisms. A special focus was set on PsP derived from fungi and insects and important industrial applications in the field of food biotechnology. The degradation of gluten and collagen as well as the hydrolysis of bitter peptides are discussed.
authors.affiliation: Institute of Food Chemistry and Food Biotechnology, Justus Liebig University Giessen, Heinrich Buff-Ring 58, 35392, Giessen, Germany.
authors.forename: Nicole
authors.initials: N
authors.lastname: Mika
authors.forename: Holger
authors.initials: H
authors.lastname: Zorn
authors.forename: Martin
authors.initials: M
authors.lastname: Rühl
mesh_terms: D005524:Food Technology; D005656:Fungal Proteins / Q000737:chemistry*; D006868:Hydrolysis; D019476:Insect Proteins / Q000737:chemistry*; D010447:Peptide Hydrolases / Q000737:chemistry*
chemical_list: D005656:Fungal Proteins; D019476:Insect Proteins; D010447:Peptide Hydrolases