Elsevier

Food Chemistry

Volume 129, Issue 2, 15 November 2011, Pages 235-244
Food Chemistry

Review
Angiotensin-I-converting enzyme and prolyl endopeptidase inhibitory peptides from natural sources with a focus on marine processing by-products

https://doi.org/10.1016/j.foodchem.2011.04.081Get rights and content

Abstract

Like many natural resource-based processing industries, the seafood processing sector gives rise to a significant volume of organic waste. Environmental issues, economic concerns and legal restrictions regarding the disposal of processing wastes have led to increased research in the discovery of alternative value-added products, such as bioactive peptides from these waste streams. Bioactive peptides have various physiological functionalities in the human body following consumption and these include antihypertensive, antiamnesiac, mineral-binding, immunodulatory, antioxidative and antithrombotic activities. The search for bioactive peptides from a variety of different sources has become a major area of research with potential for the functional foods sector. The isolation of bioactive peptides typically involves the hydrolysis of the protein of choice with different proteolytic enzymes, alone or in combination with Generally Recognised as Safe (GRAS) micro-organisms.

This review details information on angiotensin I-converting enzyme (ACE) and prolyl endopeptidase (PEP) inhibitors derived from natural, marine and marine processing waste streams and their potential for use as high-value added bioactive peptides.

Highlights

► Review of ACE-I and PEP inhibitory peptides from natural sources. ► ACE-I and PEP inhibitors from marine sources are described. ► Isolation and characterisation of ACE-I and PEP inhibitory peptides are outlined. ► Potential for high-value bioactive peptides from marine processing waste streams.

Introduction

In recent years, over-exploitation of fishery resources has become a major concern worldwide. According to data published by the Food and Agriculture Organisation (FAO), approximately 77% of the 143.6 million tons of fish and shellfish caught in 2006 was used for human consumption. The remaining processing leftovers which, includes trimmings, fins, frames, heads, shells, skin and viscera are normally used for the production of fishmeal, fish oil, fertiliser, fish silage and animal feed. These by-products may be identified as processing leftovers that are not normally saleable but which can be recycled after treatment. Annual discard from marine capture and aquaculture fisheries worldwide is estimated to be approximately 20 million tonnes per year (FAO, 2008). In Ireland, figures from An Bord Iascaigh Mhara (BIM; The Irish Sea Fisheries Board), estimated that 63,786 tonnes of marine processing waste were produced nationally in 2000, 45% of which arose from the northwest region (Pfeiffer, 2003). European legislation, Council Directive 1999/31/EC of 26 April 1999 on the landfill of waste, has set specific targets for the amount of municipal waste allowed for disposal at landfills. Landfill is also a costly waste disposal option for the seafood industry. Generation of substantial quantities of marine processing by-products is therefore both an environmental and economic concern for the seafood processing sector (Kim & Mendis, 2006). As a result, there has been increased interest in exploring the possible uses of fish by-products, or rest raw material, so that they become viewed as a potential resource due to their valuable protein and lipid content and sugars and minerals instead of a waste problem (Akihisa et al., 2004, Bruyere et al., 2004, Kelley, 2001, Larsen et al., 2000, Yokoyama et al., 1992).

Proteins from food are sources of numerous bioactive peptides with anti-hypertensive, opioid, anti-thrombotic and immunomodulating activities. The use of fish processing by-products as substrate provides a novel approach for the potential discovery of high-value bioactive products. In the past twenty years, an emerging area of research is the identification of bioactive compounds that may be present in marine by-products. Bioactive compounds are described as ‘food-derived components’ that, in addition to their nutritional value, exert a physiological effect in the body (Vermeirssen, van Camp, & Verstraete, 2004). This review aims to collate information on ACE-I-inhibitory and PEP inhibitory peptides, the isolation and characterisation strategies used to obtain these inhibitors from natural sources, with a focus on marine substrates. It also details the potential health benefits of these peptides and their potential for use as functional food components.

Section snippets

Function of ACE-I and PEP inhibitory peptides

Hypertension is one of the most common cardiovascular diseases worldwide. Data gathered by Kearney, Whelton, Reynolds, Muntner, and He (2005) demonstrated that over 25% of the adult population nearly one billion people worldwide suffer from hypertension. Hypertension is a risk factor for arteriosclerosis, stroke, myocardial infarction and end-stage renal disease (Kearney et al., 2005). The prevalence of high blood pressure increases with age, affecting approximately 65% of the population in

Sources of ACE-I and PEP inhibitory peptides

ACE-I-inhibitory peptides have been isolated from various marine proteins such as Heshiko, a fermented mackerel product (Itou & Akahane, 2004), skipjack tuna muscle (Kohama et al., 1988), sardine muscle (Bougatef et al., 2008), shark meat (Wu et al., 2008), Alaskan Pollack skin (Byun & Kim, 2001), marine shrimps (Wang et al., 2008a), pacific hake (Cinq-Mars & Li-Chan, 2007) and salmon chum (Ono, Hosokawa, Miyashita, & Takahashi, 2005) (Table 1). Theodore and Kristinsson (2007) generated a

Derivatisation of ACE and PEP inhibitory peptides

The experimental strategy for the derivatisation of ACE-I and PEP inhibitory peptides is outlined in Fig. 2. This approach employs the proteolysis of a protein source using bioassay-guided fractionation and separation of peptides followed by chemical elucidation and in vivo assays of active peptide fractions. Three key factors are important in relation to the release of peptides with bioactivities such as ACE-I and PEP inhibition. These three factors are (a) the nature of the matrices, (b) the

Structural properties involved in ACE-I and PEP inhibitory activities of peptides

It has been demonstrated that di- or tri-peptides, especially those with C-terminal proline or hydroxyproline residues, are generally resistant to degradation by digestive enzymes (Matsufuji et al., 1994, Vermeirssen et al., 2004). In addition, short peptides consisting of two or three amino acids are absorbed more rapidly than free amino acids (Gardner, 1988, Webb, 1990). The ACE inhibitory tripeptides IPP and VPP, for example, were detected in the aorta of Spontaneously Hypertensive Rats

Bioactive peptides as functional foods

Functional Foods are regulated by Regulation (EC) No. 1924/2006, of the European Parliament and of the Council, December 20, 2006: nutrition and health claims made on foods. This legislation regulates nutritional and or health claims proposed for new products, including their presentation, labelling and promotion. Japan was the first country to adopt a legal system in relation to allowable health claims on functional foods through the introduction of the FOSHU (Foods for Specific Health Use)

Conclusions

Like many natural resource-based processing industries, the seafood processing sector gives rise to a significant volume of organic waste. With EU regulations now restricting the disposal of processing wastes at sea and the ban on salmon waste from aquaculture re-entering the food chain as aquaculture feed, options available to the processing sector for legitimate waste disposal are limited. Maximising profitability from the available supply of raw material is recognised as a priority for the

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