Bioactive peptides enzymes

Surfactants, Detergents, and Enzymes Bioactive peptides, lytic enzymes, anionic surfactants Biodispersants and Biodetergents... 

Subsequent to the extensive medicinal chemistry exploration of Orexin antagonism, its utility in the treatment of sleep disorders in man has been reported recently. This important milestone for the therapeutic validation of the target results from the 0X1 /OX2 receptor antagonist ACT-078573 (20) [57], SB-649868 has also been announced to be in phase II clinical development, but neither the structural formula nor the results have been reported to date [58,59]. Moreover, insomnia treatments based on orexin modulation may be addressed by not only receptor antagonism but by inhibition of pathways related to the genesis of the bioactive peptides Orexin A or B, e.g. inhibition of Orexin-converting enzyme [60]. 

Matsui T, Li CH, Osajima Y. (1999) Preparation and characterization of novel bioactive peptides responsible for angiotensin 1-converting enzyme inhibition from wheat germ. J Pept Sci 5 289-297. 

It is more difficult to prepare a chiral a,a-dialkylammo acid. Nevertheless, when such analogues are incorporated into the backbone of a peptide chain, analogues with modified properties are obtained. In this context, such residues have been evaluated as a new type of conformational constraint for the synthesis of enzyme-resistant agonists and antagonists of bioactive peptides. Here, the asymmetric synthesis or the resolution of the chiral quaternary amino acid is necessary and numerous procedures, which have recently been reviewed, were developed to produce the requisite amino acids in enantiomerically pure form. 

Mollusks along with the crustaceans are also widely sought to participate in the world s consumption of marine food. Fermented marine food sauces such as blue mussel sauce and oyster sauce possess bioactive peptides which play a major role as Angiotensin I converting enzyme inhibitors that indirectly suppress hypertension (Wijesekara and Kim, 2010). Hence, the mollusk-derived proteins and other macromolecules are highly valuable to indicate these organisms as medicinally valuable food sources. 

Bioactive peptides can be extracted and purified with these technologies, which vary from simple to complex. Following this, the isolation of bioactive peptides, oligosaccharides, fatty acids, enzymes, water-soluble minerals, and biopolymers for biotechnological and pharmaceutical applications is possible. Further, some of these bioactive peptides have been identified to possess nutraceutical potentials that are beneficial for human health. 

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... 

Marine fishes are rich sources of structurally diverse bioactive compounds including polyunsaturated fatty acids, polysaccharides, minerals, vitamins, antioxidants, enzymes, and bioactive peptides (Kim et ah, 2008). Marine fish-derived ACE inhibitory peptides have been purified from enzymatic digestion of various fish materials from Alaska pollack (Nakajima et ah, 2009), bonito (Fujita et ah, 2000 Hideaki et ah, 1993 Yokoyama et ah,... 

The discovery of a multitude of naturally occurring, bioactive peptides has generated a rich source of pharmacophores from which medicinal chemists are developing new useful therapeutic drugs. After binding to an enzyme, or a membrane receptor, peptide-based inhibitors, neurotransmitters, immunomodulators, and hormones influence cell-to-cell communications and control a variety of vital functions such as metabolism, immune defense, digestion, respiration, sensitivity to pain, reproduction, and behavior. 

Many biological cells contain degradative enzymes (proteases) that catalyze the hydrolysis of peptide linkages. In the intact cell, functional proteins are protected from these destructive enzymes because the enzymes are stored in cell organelles (lysosomes, etc.) and released only when needed. The proteases are freed upon cell disruption and immediately begin to catalyze the degradation of protein material. This detrimental action can be slowed by the addition of specific protease inhibitors such as phenylmethyl-sulfonyl fluoride or certain bioactive peptides. These inhibitors are to be used with extreme caution because they are potentially toxic. 

The influence of eutectic media on the kinetics and productivity of biocatalysts has yet to be fully elucidated. Syntheses in eutectic suspensions have been scaled up to the pilot scale in a rotating drum reactor. The bioactive peptide Na-Cbz-L-Lys(Ne-Cbz)-Gly-L-Asp(OAll)-L-Glu(OAll)OEt was synthesized via a sequential N-to-C strategy in a heterogeneous solid-liquid mixture of the substrates in the presence of chymopapain and subtilisin as well as 16-20% (w/w) water and ethanol (Gill, 2002). At substrate concentrations of around 1 m, yields of 67-74% per step at product concentrations of 0.36, 0.49, and 0.48 kg kg-1 were achieved. The corresponding space-time yields were between 0.30 and 0.64 kg (kg d)-1 and biocatalyst reuse provided productivities of 166-312 kg product (kg enzyme)-1. 

Smacchi, E. and Gobetti, M. 2000. Bioactive peptides in dairy products synthesis and interaction with proteolytic enzymes. Food Microb. 17, 129-141. 

Pancreatic enzymes, preferably trypsin, have been used for the chemical characterisation and identification of many known bioactive peptides. For example, ACE-inhibitory peptides as well as CPPs are most commonly produced by trypsin (Maruyama and Suzuki, 1982 Berrocal et al., 1989). On the other hand, other enzymes and different enzyme combinations of proteinases, including alcalase, chymotrypsin, pancreatin and pepsin, as well as enzymes from bacterial and fungal sources have also been utilised to generate bioactive peptides. Higher yields of CPPs and, particularly, higher amounts of asl-casein f(59-79) in the hydrolysate have been obtained with casein micelles successively digested with pepsin and trypsin... 

RELEASE OF BIOACTIVE PEPTIDES FROM MILK PROTEINS BY VARIOUS MICROORGANISMS AND MICROBIAL ENZYMES... 

Haileselassie, S.S., Lee, B.H., and Gibbs, B.F. 1999. Purification and identification of potentially bioactive peptides from enzyme-modified cheese. J. Dairy Sci. 82(8), 1612-1617. 

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