Work

Pancreatic lipase exhibits selective esterase activity on carboxyl-linked hydroxycinnamic acid glucosides

Year: 2025

Type: article

Abstract: This study explores the susceptibility of phenolic acids (PAs) to digestion. 24 PAs were identified in apple, including 6 hydroxybenzoic acids (HBAs) and 18 hydroxycinnamic acids (HCAs), most of which were derivatives. PA derivatives showed distinct digestion patterns, clustering into groups. Group 1, with HBAs and HCAs esterified to glucose, had lower bioaccessible concentrations after the intestinal phase than Group 2, which included HCAs esterified to quinic acid or glycosylated via a β-O-glycosidic bond. Under different digestion conditions, the β-O-glycosidic bonds in ferulic acid 4-O-β-D-glucoside (FAG) and 4-hydroxybenzoic acid 4-O-β-D-glucoside resisted hydrolysis, while 6-O-feruloyl-d-glucose (FG), linked by an ester bond, was hydrolysed by pancreatin. When FG and its isomer FAG were digested with individual pancreatic enzymes (amylase, trypsin or lipase), FAG remained intact, whereas FG was hydrolyzed by lipase, mirroring pancreatin. Findings indicate a specific esterase activity of pancreatic lipase on HCAs esterified to glucose via a carboxyl ester bond.

Source: Food Chemistry

DOI: 10.1016/j.foodchem.2025.144939

Authors: Ivan M. Lopez-Rodulfo, Pablo Gallego-Lobillo, Mario M. Martinez

Institutions: Aarhus University, Universidad de Valladolid

Language: English

Topic: Phytochemicals and Antioxidant Activities

Subfield: Biochemistry

Field: Medicine

Domain: Health Sciences

Open Access status: hybrid

Estimated APC paid: $4,930

Funders: Aarhus Universitet, Fundación Alfonso Martín Escudero, Sundhed og Sygdom, Det Frie Forskningsråd, Danmarks Frie Forskningsfond