The effects of combined enzymatic and physical modifications of lentil protein applying Alcalase, Flavourzyme, microbial transglutaminase, and ultrasound: antioxidant, antihypertension, and antidiabetic activities

• Published in: Journal of food measurement & characterization 2022-10, Vol.16 (5), p.3743-3759
• Main Authors: Rezvankhah, Amir, Yarmand, Mohammad Saeid, Ghanbarzadeh, Babak
• Format: Article
• Language: English
• Subjects: Amino acid composition; Amino acids; Amylases; Angiotensin; Antioxidants; Centrifugation; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Crosslinking; Diabetes mellitus; Electrophoresis; Engineering; Food Science; Gel electrophoresis; Glucosidase; Hydrolysates; Hydrolysis; Hydrophobicity; Liquid chromatography; Microorganisms; Molecular weight; Molecular weight distribution; Original Paper; Peptides; Peptidyl-dipeptidase A; Polyacrylamide; Proteins; Reduction; Scavenging; Sodium lauryl sulfate; Sonication; Subtilisin; Ultrasonic imaging; Ultrasonic processing; Ultrasound; α-Amylase; α-Glucosidase
• ISSN: 2193-4126; 2193-4134
• DOI: 10.1007/s11694-022-01478-z

The enzymatically and physically modified lentil protein (LP) was assessed for antioxidant, antihypertension, and antidiabetic activities. First, Alcalase and Flavourzyme were sequentially used to produce lentil protein hydrolysate (LPH). Then, the LPH underwent microbial transglutaminase (MTGase)-mediated cross-linking (LPHC) and ultrasound treatment (LPHUS) individually and combinatory (LPHUSC). The amino acid composition, surface hydrophobicity ( H 0 ), molecular weight (MW) profile and distribution, DPPH and ABTS radical scavenging activities (RSA), angiotensin-converting enzyme I-inhibitory (ACE), α-amylase, and α-glucosidase inhibitory activities, and functional properties were investigated. Results showed that the amino acid profiles were maintained after hydrolysis, cross-linking, and sonication while the residual values were slightly altered due to the centrifugation stages. Hydrolysis exposed the buried hydrophobic patches which led to a significant increase in H 0 while cross-linking reburied them which caused a remarkable reduction in H 0 ; Ultrasound also indicated a slight reducing effect in H 0 . Sodium dodecyl sulfide polyacrylamide gel electrophoresis (SDS-PAGE) and gel permeation chromatography (GPC) results indicated that hydrolysis remarkably decreased the MW, cross-linking had an enlarging effect on peptides, and ultrasound disrupted the formed aggregates during hydrolysis. The hydrolysis increased DPPH and ABTS RSA while cross-linking had a decreasing effect on DPPH RSA and a slight increasing effect on ABTS RSA; Ultrasound indicated a slight reduction in DPPH RSA. The highest ACE, α-amylase, and α-glucosidase inhibitory activities were obtained for LPHC and LPHUSC. Also, LPHUSC indicated higher emulsifying activity and moderate stability. Consequently, LPHC and LPHUSC could be introduced as a potent mixture of peptides with antioxidant, antihypertension, and antidiabetic activities.