Biological activities of whey protein hydrolysate produced by protease from the Antarctic bacterium Lysobacter sp. A03. (August 2022)

• Record Type: Journal Article
• Authors: Millan, Gersi Cristina Lunar; Veras, Flávio Fonseca; Stincone, Paolo; Pailliè-Jiménez, Maria Elisa; Brandelli, Adriano
• Is Part Of: Biocatalysis and agricultural biotechnology. Number 43(2022)
• Publication Date: 2022-08
• Subjects: Whey -- Cold active protease -- Protein hydrolysate -- Bioactive peptide -- Antioxidant activity -- Antihypertensive activity; Agricultural biotechnology -- Periodicals; Enzymes -- Biotechnology -- Periodicals; 660.6
• DOI: 10.1016/j.bcab.2022.102415
• Languages: English
• ISSNs: 1878-8181

Abstract

Abstract: Several biological activities have been related to peptides derived from food proteins. Short peptides encrypted within the original protein sequence can be released by the action of proteolytic enzymes, exerting several biological activities that can be useful in food preservation and as nutraceutical compounds. In this study, bovine whey hydrolysates were produced using the protease from Lysobacter sp. A03, a psychrotolerant bacterium from Antarctica. The antioxidant activity increased during whey protein hydrolysis, reaching radical scavenging values around 47% and 11% for ABTS (2, 2′-azinobis (3-ethylbenzothiazoline-6-sulfonic acid)) and DPPH (2, 2-diphenyl-1-picryl-hydrazyl), respectively. The iron chelating capacity and TBARS values were high for non-hydrolyzed whey (about 69% and 87%, respectively), with no clear relationship with the hydrolysis time. A significant increase of antihypertensive activity, estimated by inhibition of the angiotensin-I-converting enzyme (ACE), was recorded in 2 h reaching values about 91%. Bioactive peptides were predicted by in silico hydrolysis of major whey proteins using the BIOPEP-UWM database and de novo annotation after mass spectrometry analysis. This study indicates the potential of Lysobacter A03 protease to produce protein hydrolysates with antioxidant and antihypertensive activity. Highlights: Hydrolysis of whey proteins by protease of cold-active Lysobacter sp. Whey hydrolysates presented antioxidant and antihypertensive activities. Bioactive peptides predicted by in silico hydrolysis and database searching. Cold-active proteases may be beneficial to produce bioactive whey hydrolysates.