Peptides, from marine sources

TABLE 27.1. Partial list of ACE inhibitory peptides from marine sources. 

Aneiros, A. and Garateix, A. (2004). Bioactive peptides from marine sources Pharmacological properties and isolation procedures. /. Chromatogr. B 803, 41-53. 

As antioxidant peptides are rarely present in marine invertebrates, they must be released from the parent protein by hydrolysis with enzymes. Various enzymes have been used to release peptides from muscle proteins. To date, different muscle proteins have been extracted, hydrolysed, and their antioxidant activities studied, which is among all invertebrate muscles the most similar to vertebrate skeletal muscle. Various studies have been conducted to investigate the antioxidant properties of hydrolysates or bioactive peptides from marine invertebrate sources like oysters... 

This suggests that products with bioactive peptides derived from marine invertebrates can meet the needs of marine organism-derived products due to health and/or religious reasons. From such a viewpoint, hydrolysates or bioactive peptides from marine invertebrates can be interesting sources of bioactivity peptides in the treatment of chronic diseases. 

Anti-HIV compounds from marine sources also included terpenoids, steroids, peptides and alkaloids. Avarol, Fig. (1) and avarone. Fig. (2), sesquiterpenoid hydroquinones from the marine sponge Dysidea cinerea, are promising anti-HIV compounds [41,42]. Three new... 

Nowadays, ACE inhibitory peptides have been isolated from meat, remaining muscle proteins, skin collagen and gelatin, bone, and internal organs of fishes such as Alaska pollack, bonito, tuna, salmon, shark, and sardine. Table 16.1 provides a partial summary of ACE inhibitory peptides derived from marine fish sources, their amino acid sequence, the enzyme used for hydrolysis, and IC50 values. The IC50 value is the concentration of peptide that inhibits 50% of ACE activity. 

TABLE 16.1 ACE inhibitory peptides derived from marine fish source, enzyme used for hydrolysis, amino acid sequence and IC50 value... 

N-Alkylation is an important modification of the peptide bond. In particular, N-methylation is widespread and commonly occurs in natural peptides from plants, marine sources, and various microorganisms. Several of these compounds have important biological activity, such as antibiotic (e.g., enniatins, 1 monamycins, 2 echinomycin 3 ), antitumor (e.g., bouvardin, 4 dolastatin 56 ) and immunosuppressor activity (e.g., cyclosporin 7 ). For reviews see refs 8-10. ... 

Food materials, including fish, contain the precursors to these bioactive peptides, which can be formed in vitro or in vivo by enzymatic hydrolysis (Korhonen and Pihlanto 2003). During the past decade, a number of studies have reported on the many physiological properties of these bioactive peptides. The aim of this review is to describe the production of novel peptides derived from marine protein hydrolysates, elucidating the underlying mechanisms of physiological and biofunctional activity that are particular to individual bioactive peptides. The general sources and production of protein hydrolysates will be discussed, followed by a discussion of the nutraceutical properties of protein hydrolysates and their associated bioactive peptides. 

Generally speaking, the peptide toxins from marine animal sources are more natural product-like than their terrestrial counterparts, as on average they are smaller in size and more heavily modified. For this reason, in this chapter, we will concentrate on the peptide toxins expressed by cone snails and sea anemones as quintessential examples of natural peptide toxins suitable for therapeutic uses. 

The bioactIve secondary metabolites from several marine sources, sponges and tunica-tes (Kobayashl/lshibashi), sea plumes (Katz/Adamczeski) and ascidians (Bowdem) cover a broad range of different chemical structures, terpenoids, unsaturated fatty acids, steroids, alkaloids, cyclic peptides and polysaccharides. 

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