Food Biochemistry and Food Processing (2 edition)

BLBS102-c36 BLBS102-Simpson March 21, 2012 18:47 Trim: 276mm X 219mm Printer Name: Yet to Come

36 Biological Activities and Production of Marine-Derived Peptides 689

Table 36.2.Source, Amino Acid Sequence and Molecular Weight of Antioxidative Peptides from Some Aquatic

Protein Hydrolysates

Sources Enzymes Da Peptide Sequence References

Tuna cooking juice Protease XXIII 751 Pro–His–His–Ala–Asp–Ser Jao and Ko (2002)

Yellowfin sole frame Pepsin, Mackerel

intestine crude enzyme

1300 Arg–Pro–Asp–Phe–Asp–Leu–Glu–

Pro–Pro–Tyr

Jun et al. (2004)

Alaska Pollack frame Mackerel intestine crude

enzyme

672 Leu–Pro–His–Ser–Gly–Tyr Je et al. (2005c)

Giant squid muscle Trypsin 747 Asn–Gly–Leu–Glu–Gly–Leu–Lys Rajapakse et al. (2005b)

1307 Asn–Ala–Asp–Phe–Gly–Leu–Asn–

Gly–Leu–Glu–Gly–Leu–Ala

Jumbo squid skin gelatin Trypsin 880 Phe–Asp–Ser–Gly–Pro–Ala–Gly–

Va l – L e u

Mendis et al. (2005b)

1242 Asn–Gly–Pro–Leu–Gln–Ala–Gly–

Gln–Pro–Gly–Glu–Arg

Hoki skin gelatin Trypsin 797 His–Gly–Pro–Leu–Gly–Pro–Leu Mendis et al. (2005a)

Conger eel Tryptic enzyme 928 Leu–Gly–Leu–Asn–Gly–Asp–Asp–

Val–Asn

Ranathunga et al. (2006)

Tuna backbone Pepsin 1519 Val–Lys–Ala–Gly–Phe–Ala–Trp–

Thr–Ala–Asn–Gln–Gln–Leu–Ser

Je et al. (2007)

Hoki frame Pepsin 1801 Glu–Ser–Thr–Val–Pro–Glu–Arg–

Thr–His–Pro–Ala–Cys–Pro–Asp–

Phe–Asn

Kim et al. (2007)

Oyster protein Pepsin 1600 Leu–Lys–Gln–Glu–Leu–Glu–Asp–

Leu–Leu–Glu–Lys–Gln–Glu

Qian et al. (2008b)

Bigeye tuna dark muscle Pepsin 1222 Leu–Asn–Leu–Pro–Thr–Ala–Val–

Tyr–Met–Val–Thr

Je et al. (2008)

Tuna cooking juice Orientase 1305 Pro–Val–Ser–His–Asp–His–Ala–Pro–

Glu–Tyr

Hsu et al. (2009)

938 Pro–Ser–Asp–His–Asp–His–Glu

584 Val–His–Asp–Tyr

Sardinelle (head,

viscera)

Crude extract from

sardine viscera

431 Leu–His–Tyr Bougatef et al. (2010)

Tuna dark muscle

by-product

Protease XXIII 756 Pro–Met–Asp–Tyr–Met–Val–Thr Hsu (2010)

978 Leu–Pro–Thr–Ser–Glu–Ala–Ala–

Lys–Tyr

Loach muscle Papain 464 Pro–Ser–Tyr–Val You et al. (2010)

causes of many serious human diseases, such as cardiovascu-

lar disease, cancer, and neurological disorders as well as the

aging process (Jittrepotch et al. 2006). To prevent foods from

undergoing oxidative deterioration and to provide protection

against serious diseases, it is important to inhibit the oxidation

of lipids and formation of free radicals occurring in the living

body and foodstuffs. In this regard, several antioxidants have

been used to maintain food quality. Also, there is keen interest

in antioxidants from natural sources for use as food supple-

ments or processing aids. The commonly used antioxidants are

chemically synthesized antioxidants such as butylated hydrox-

yanisole, butylated hydroxytoluene, tert-butylhydroquinone, etc.

However, these antioxidants are suspected to pose toxicity prob-

lems in the long term and their use in foodstuffs is restricted

or prohibited in some countries (Sakanaka et al. 2004, Je et al.

2005a, Pihlanto et al. 2008).

Recently, a number of studies have demonstrated that pep-

tides derived from different marine animal protein hydrolysates

act as potent antioxidants (Table 36.2). Some of these antioxi-

dant peptides have exhibited varying capacities to scavenge free

radicals. Several studies have indicated that peptides derived

from marine fish proteins have greater antioxidant properties

thanα-tocopherol in different oxidative systems (Jun et al. 2004,

Rajapakse et al. 2005b). However, the exact mechanism of ac-

tion of bioactive peptides as antioxidants is not clearly known.

Some peptides are capable of chelating metal ions, which acts

as the pro-oxidant (Klompong et al. 2007). The antioxidant ac-

tivity of protein hydrolysates has been attributed to the presence

of certain amino acids in the peptide sequence. High amounts of

histidine and some hydrophobic amino acids are related to the

antioxidant potency. Davalos et al. (2005) indicated that trypto- ́

phan, tyrosine and methionine showed the highest antioxidant