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

688 Part 6: Health/Functional Foods

Table 36.1.Angiotensin Converting Enzyme (ACE) Inhibitory Peptides Derived from Fishery Sources

Source Enzyme Peptide Sequence IC 50 Va l u ea References

Tuna frame Peptic enzymes Gly–Asp–Leu–Gly–Lys–Thr–Thr–

Thr–Val–Ser–Asn–Trp–Ser–Pro–

Pro–Lys–Try–Lys–Asp–Thr–Pro

11.28μM Lee et al. (2010)

Shark meat Protease Cys–Phe 1.96μM Wu et al. (2008)

Glu–Tyr 2.68μM

Phe-Glu 1.45μM

Bigeye tuna dark

muscle

Pepsin Trp–Pro–Glu–Ala–Ala–Glu–Leu–

Met–Met–Glu–Val–Asp–Pro

21.6μM Qian et al. (2007)

Anchovy natural fermentation Arg–Pro 21 μM Ichimura et al. (2003)

Lys–Pro 22 μM

Ala–Pro 29 μM

Salmon Thermolysin Val–Trp 2.5μM Ono et al. (2003)

Ile–Trp 4.7μM

Met–Trp 9.9μM

Leu–Trp 17.4μM

Cuttlefish Bacterial protease Ala–His–Ser–Tyr 11.6μM Balti et al. (2010a)

Gly–Asp–Ala–Pro 22.5μM

Ala–Gly–Ser–Pro 37.2μM

Asp–Phe–Gly 44.7μM

Cuttlefish Proteases Val–Tyr–Ala–Pro 6.1μM Balti et al. (2010b)

Val–Ile–Ile–Phe 8.7μM

Met–Ala–Trp 16.32μM

Shrimp Peptide enzymes Leu–His–Pro 1.6μM Cao et al. (2010)

Shrimp Lactobacillus fermentum

enzymes

Asp–Pro 2.15μM Wang et al. (2008b)

Gly–Thr–Gly 5.54μM

Ser–Thr 4.03μM

Hard clam Protamex Tyr–Asn 51 μM Tsai et al. (2008)

Oyster Pepsin Val–Val–Tyr–Pro–Trp–Thr–Gln–

Arg–Phe

66 μM Wang et al. (2008a)

Freshwater clam Protamex and

flavourzyme

Val–Lys–Pro 3.7μM Tsai et al. (2006)

Val–Lys–Lys 1045 μM

Blue mussel Natural fermentation Glu–Val–Met–Ala–Gly–Asn–Leu–

Tyr–Pro–Gly

19.34μg/mL Je et al. (2005d)

aIC 50 value is defined as the concentration of inhibitor required to inhibit 50% of the ACE activity.

pressure by 11 mm Hg, while the control group showed no

decrease. Lee et al. (2010) reported that a single oral administra-

tion (10 mg/kg of body weight) of peptide from tuna frame hy-

drolysate displayed a strong suppressive effect on systolic blood

pressure of SHR and this antihypertensive activity was similar to

captopril. Moreover, no adverse side effects were observed in the

rats after administration of antihypertensive peptide. Although,

the exact mechanisms underlying this phenomenon have not yet

been identified, it was suggested that bioactive peptides have

higher tissue affinity and are subjected to a slower elimination

than captopril.

Currently, protein hydrolysates from the bonito and sardine

are widely available as supplements in Japan (Guerard et al. ́

2010). Bonito hydrolysate is also being sold in North Amer-

ica as a supplement to lower blood pressure. Similar products

have been derived from other proteins, including soy and whey.

However, active dosages in these nonmarine products are 1020

g/day, whereas bonito protein hydrolysis, for example, has a

recommended daily dosage of only 1.5 g/day. A low daily dose

is important for both ingredient cost and ease of formulation.

Marine-derived bioactive peptides have potential for use as func-

tional ingredients in nutraceuticals and pharmaceuticals due to

their effectiveness in both prevention and treatment of hyperten-

sion. However, further studies are needed with clinical trials for

these antihypertensive peptides.

Antioxidant Activity

Lipid oxidation is one of the major deteriorations in many types

of natural and processed foods, leading to changes in food

quality and nutritional value and also production of potentially

toxic reaction products. Furthermore, lipid oxidations are major