Abstract
The current objective was framed on isolation of two angiotensin-I converting enzyme inhibitory peptides from coastal trashes of squilla muscle (Harpiosquilla raphidea) prepared by enzymatic hydrolysis using alcalase, thermolysin and trypsin, which showed the highest degree of hydrolysate in 12th h hydrolysate 87.9 ± 1.6%, 63.1 ± 1.1% and 91.1 ± 2.7% respectively. Among these three hydrolysates, alcalase 5th h (64.8 ± 0.3) and thermolysin 6th h (68.4 ± 1.0) found to be maximum ACE-I inhibition activity. Initial separation was performed by ultra filtration (10–3 kDa) into three different fractions, alcalase (below 3 kDa) fraction observed maximum ACE-I inhibition activity with 75.2 ± 3.5% and thermolysin (3–10 kDa) with 79.5 ± 1.0% inhibition. Further, these two fractions have taken to ion exchange and gel filtration chromatography, the identified ACE-I inhibitory fractions (AC-A2 and TH-A2) also examined for its antioxidant properties. Further, these fractions were determined to be non-toxic against cell lines, functional activities by various assays and characterized into tri peptides MSN (Met-Ser-Asn) and MTH (Met-Thr-His) with a molecular weight of 350 Da and 388 Da respectively using LC–MS/MS. These low molecular weight peptides from natural sources may act as potential ingredient for nutraceutical and pharmaceutical industries.
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Acknowledgements
This research was supported by a grant No: SB/YS/LS-328/2013 funded by the Department of Science and Technology (DST)—Science & Engineering Research Board (SERB) of the government of India. We extend our gratitude to the management and SRM Institute of Science and Technology for providing the facilities.
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Noorani, K.P.M., Nazeer, R.A. Enzymatic Production of Two Tri-peptides on ACE-I Inhibition and Antioxidant Activities. Int J Pept Res Ther 26, 2365–2377 (2020). https://doi.org/10.1007/s10989-020-10037-3
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DOI: https://doi.org/10.1007/s10989-020-10037-3