Abstract

ABSTRACTLiposomes are used as effective nanodelivery devices to improve the physicochemical stability and biological efficacy of the encapsulated peptides and proteins. In this study, nanoliposome composite of lipoid S75-entrapped angiotensin I-converting enzyme (ACE)-inhibitory biopeptides was prepared by conventional (BLS75-CM) and direct heating (BLS75-DHM) methods. The nanoliposomes (BLS75-CM and BLS75-DHM) were stored at 4°C for 8 weeks and evaluated for physicochemical stability in terms of particle size, polydispersity index (pdi), zeta potential, and encapsulation efficiency (EE). These were also studied for residual ACE-inhibitory efficacy following their digestion under simulated gastrointestinal tract condition. The BLS75-CM was found to maintain higher physicochemical stability in terms of particle size, pdi, and zeta potential compared to BLS75-DHM. However, the BLS75-DHM indicated higher EE and efficacy with greater residual ACE-inhibitory activity of 47.37% compared to 44.18% and 36.84% that were obtained for the digested BLS75-CM and digested biopeptides without encapsulation, respectively. In vitro release study showed a cumulative biopeptides release of 66.41% and 69.00% from BLS75-CM and BLS75-DHM, respectively. The results of transmission electron microscopy showed spherical appearance of the nanoliposome capsules while Fourier Transform Infrared spectroscopy indicated the presence of ionic complexation and hydrogen bonds between the biopeptides and their phospholipid matrix.

Highlights

  • The nanoliposomes containing stone fish-derived angiotensin I-converting enzyme (ACE)-inhibitory biopeptides were prepared by conventional method (CM) and direct heating method (DHM) and evaluated for physicochemical stability and Transmission electron microscopy (TEM)

  • The residual ACE-inhibitory activity was determined to assess the efficacy of the biopeptides being released from the nanoliposome capsules subjected to in vitro gastrointestinal digestion under simulated-gastric fluid (SGF) and simulated-intestinal fluid (SIF), respectively

  • The physicochemical stability of the nanoliposomes-entrapped ACE-inhibitory biopeptides was evaluated by measuring the changes in EE, particle size, pdi, and zeta potential once per week during the 8 weeks of storage at 4°C

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Summary

Introduction

Enzymatic hydrolysis of food protein generates biologically active peptides of short amino acids sequences with diverse physiological benefits. [1,2,3] Bioactive peptides with strong antioxidants and angiotensin I-converting enzyme (ACE)-inhibitory activity have been produced from different food sources, [4,5,6] and can be incorporated into different food products to reduce the risk of certain lifethreatening diseases like hypertension and diabetes or to supplement demand for patients diagnosed with specific clinical conditions including acute and chronic liver disease, pancreatitis, phenylketonuria, and ulcerative colitis. [7] orally administered peptides exhibit low stability in the gastrointestinal tract (GIT) and can be degraded. [7] orally administered peptides exhibit low stability in the gastrointestinal tract (GIT) and can be degraded This together with their low intestinal permeability may render them ineffective with low bioavailability and biological efficacy. The biopeptides generated from stone fish protein were proven to be potent antioxidant and ACEinhibitory molecules [28,29] and can be used as a source of soluble peptides for protein enrichment of food and beverages. Their low stability against digestive enzymes and during storage together with an unpleasant odor may limit the direct use of stone fish biopeptides as bioingredients for food formulation.

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