72
was not affected after incubation with proteases. This ACE inhibitor had a clear
antihypertensive effect in spontaneously hypertensive rats, at a dosage of 1 mg/kg
(Lee et al. 2004).
ACE inhibitory activity (58.7%) was detected in a cold water extract of Grifola
frondosa (IC 50 of 0.95 mg). The extraction time increased the ACE inhibitory activity. After the purification of ACE inhibitory peptides was obtained an active fraction
with an IC 50 of 0.13 mg and a yield of 0.7%. The purified peptide showed competitive inhibition on ACE and maintained its inhibitory activity even after digestion by
intestinal proteases (Choi et al. 2001).
A novel ACE inhibitory peptide (decapeptide) from Saccharomyces cerevisiae
was purified and characterized. Maximal production of the ACE inhibitor was
observed after 24 h of cultivation at 30 °C, and the activity was increased 1.5 times
after treatment of the cell-free extract with pepsin. The purified peptide showed very
low similarity to other ACE inhibitory peptide sequences, and its amino acid
sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor
had a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a
dosage of 1 mg/kg body weight (Jae-Ho et al. 2004).
The yeast Malassezia pachydermatis G-14 produced a novel ACE inhibitor when
the strain was cultured in YEPD medium containing 0.5% yeast extract, 3.0% peptone, and 2.0% glucose at 30 °C for 24 h (Jeong et al. 2005).
A novel ACE inhibitory peptide (pentapeptide) was obtained from the water
extract of the fruiting body of Pholiota adiposa ASI 24012. The purified ACE inhibitory peptide showed very low similarity to other ACE inhibitory peptide sequences.
Its molecular mass was of 414 Da with a sequence of Gly-Glu-Gly-Gly-Pro and
showed a clear antihypertensive effect on spontaneously hypertensive rats (SHR), at
a dosage of 1 mg/kg (Kyo-Chul et al. 2006).
Recently, reishi (Ganoderma lingzhi) was studied to find ACE inhibitory peptides. To obtain auto-digested reishi (ADR) extract, reishi’s protein was hydrolyzed
by its own proteases. After 4 h administration of ADR to spontaneous hypertensive
rats (SHRs), their systolic pressure significantly decreased to 34.3 mmHg (19.5%
change) and the effect was observed up to 8 h of administration, with the decrease
reaching as low as 26.8 mmHg. Eleven peptides were identified and four of them
showed potent inhibition against ACE (IC 50 values ranging from 73.1 μM to
162.7 μM) (Hai-Bang et al. 2014).
5.3 Antioxidant
Oxidative stress occurs when the production of harmful molecules, called free radicals (molecules highly unstable and reactive because they have one or more unpaired
electrons), is greater than the protective capacity of antioxidant defenses. Within the
radicals are the hydroxyl radical, superoxide anion radical, hydrogen peroxide, singlet oxygen, nitric oxide radical, and hypochlorite radical, among others; also
smoking, ionizing radiation, pollution, organic solvents, and pesticides, among
G. Díaz-Godínez and R. Díaz
was not affected after incubation with proteases. This ACE inhibitor had a clear
antihypertensive effect in spontaneously hypertensive rats, at a dosage of 1 mg/kg
(Lee et al. 2004).
ACE inhibitory activity (58.7%) was detected in a cold water extract of Grifola
frondosa (IC 50 of 0.95 mg). The extraction time increased the ACE inhibitory activity. After the purification of ACE inhibitory peptides was obtained an active fraction
with an IC 50 of 0.13 mg and a yield of 0.7%. The purified peptide showed competitive inhibition on ACE and maintained its inhibitory activity even after digestion by
intestinal proteases (Choi et al. 2001).
A novel ACE inhibitory peptide (decapeptide) from Saccharomyces cerevisiae
was purified and characterized. Maximal production of the ACE inhibitor was
observed after 24 h of cultivation at 30 °C, and the activity was increased 1.5 times
after treatment of the cell-free extract with pepsin. The purified peptide showed very
low similarity to other ACE inhibitory peptide sequences, and its amino acid
sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor
had a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a
dosage of 1 mg/kg body weight (Jae-Ho et al. 2004).
The yeast Malassezia pachydermatis G-14 produced a novel ACE inhibitor when
the strain was cultured in YEPD medium containing 0.5% yeast extract, 3.0% peptone, and 2.0% glucose at 30 °C for 24 h (Jeong et al. 2005).
A novel ACE inhibitory peptide (pentapeptide) was obtained from the water
extract of the fruiting body of Pholiota adiposa ASI 24012. The purified ACE inhibitory peptide showed very low similarity to other ACE inhibitory peptide sequences.
Its molecular mass was of 414 Da with a sequence of Gly-Glu-Gly-Gly-Pro and
showed a clear antihypertensive effect on spontaneously hypertensive rats (SHR), at
a dosage of 1 mg/kg (Kyo-Chul et al. 2006).
Recently, reishi (Ganoderma lingzhi) was studied to find ACE inhibitory peptides. To obtain auto-digested reishi (ADR) extract, reishi’s protein was hydrolyzed
by its own proteases. After 4 h administration of ADR to spontaneous hypertensive
rats (SHRs), their systolic pressure significantly decreased to 34.3 mmHg (19.5%
change) and the effect was observed up to 8 h of administration, with the decrease
reaching as low as 26.8 mmHg. Eleven peptides were identified and four of them
showed potent inhibition against ACE (IC 50 values ranging from 73.1 μM to
162.7 μM) (Hai-Bang et al. 2014).
5.3 Antioxidant
Oxidative stress occurs when the production of harmful molecules, called free radicals (molecules highly unstable and reactive because they have one or more unpaired
electrons), is greater than the protective capacity of antioxidant defenses. Within the
radicals are the hydroxyl radical, superoxide anion radical, hydrogen peroxide, singlet oxygen, nitric oxide radical, and hypochlorite radical, among others; also
smoking, ionizing radiation, pollution, organic solvents, and pesticides, among
G. Díaz-Godínez and R. Díaz