Peptidomics and molecular dynamics on bioactive peptides produced and characterized from the fermented whey of "Panchali" sheep of West India.

The study assessed the peptide production by using potent Lactiplantibacillus plantarum KGL3A (MG722814) culture to ferment the sheep milk for evaluation of α-glucosidase inhibition, ACE inhibition, α-amylase inhibition, & inhibiting lipase activities. The maximal ACE inhibitory, α-amylase, α-glucosidase, & lipase inhibiting actions were 71.69 %, 71.32 %, 67.14 %, and 64.15 %, respectively, at 37 °C after 48 h. Proteolytic activity was tested at various incubation times & inoculation rates to maximise the conditions for growth and the greatest action (9.38 mg/mL) was reported at 2.5 % rate of inoculation after incubation of 48 h. The anti-diabetic as well as ACE inhibitory properties of less than 3 kDa were maximum in contrast to >3 kDa, <10 kDa, and > 10 kDa cut-off fractions. Further, when LPS stimulation is applied to RAW 267.4 macrophage cells, the overabundance generation of IL-6, IL-1β, NO, and TNF-α is greatly reduced by using KGL3A to ferment sheep milk. 2D gel electrophoresis & SDS-PAGE were utilized in relation to protein purifications. Maximum numbers of sheep milk's fermented protein bands were present, about 10 to 124 kDa by SDS-PAGE, and 38 spots of protein were discovered using 2D gel chromatography. Ultra-filtered fractions water soluble extracts (WSEs) were employed in RP-HPLC to differentiate between various peptide fractions. The peptide sequences produced were matched using the databases of AHTPDB and BIOPEP to match hypertensive peptides & antidiabetic peptides, respectively. Furthermore, the discovered peptide sequences from the fermenting sheep milk was studied due to their penchant for binding against the active locations of human bile salt activated lipase (hBAL); human maltase-glucoamylase (hMGA); human pancreatic alpha-amylase (hPAM); & human angiotensin-converting enzyme (hACE) through molecular docking.