ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)

Tsai, Jung‐Hui; Chen, Jia-Ling; Pan, Bonnie Sun

doi:10.1016/j.procbio.2008.02.019

Cited by 135 publications

(69 citation statements)

References 32 publications

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“…Some researchers have shown some comparable results from sequenced peptides from various other sources including Gly-Phe-His-Ile and Gly-Phe-His-Ile-Asn-Gly (117 and 64.3 µg/ ml respectively) from beef muscle, Asn-Asp (1200 and 8100 µg/ml) from head and visceral of sardinelle and the same sequence from porcine meat (3.9 mg/ml) [2]. Nevertheless, comparison from various researches could be complicated as different methods might have been employed in estimating IC 50 which might have a very significant effect on the acclaimed activities [55][56][57].…”

Section: Ace Activities Of the Sec Classified Fractionsmentioning

confidence: 99%

Antioxidant and Angiotensin 1 Converting Enzyme Inhibitory Functions from Chicken Collagen Hydrolysates

Soladoye¹,

Saldo²,

Peiró³

et al. 2014

J Nutr Food Sci

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Section: Ace Activities Of the Sec Classified Fractionsmentioning

confidence: 99%

Antioxidant and Angiotensin 1 Converting Enzyme Inhibitory Functions from Chicken Collagen Hydrolysates

Soladoye¹,

Saldo²,

Peiró³

et al. 2014

J Nutr Food Sci

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“…It was observed that after digestion by pepsin and mixture of pepsin and pancreatin, ACE inhibitory potencies of fractions were almost the same as the control samples (Table 3). Wu et al (2008) and Tsai et al (2008) reported that short-chained peptides with very low molecular weights were resistant to gastrointestinal peptidases due to their fast absorption in the small intestine. The findings from present study also recommended that potent ACE inhibitory peptides extracted from P. sutchi skin and bone gelatins could possibly maintain their inhibition activity after being orally administered.…”

Section: Degree Of Hydrolysis (%)mentioning

confidence: 99%

ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

et al. 2012

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Skin and bone gelatins of pangasius catfish (Pangasius sutchi) were hydrolyzed with alcalase to isolate Angiotensin Converting Enzyme (ACE) inhibitory peptides. Samples with the highest degree of hydrolysis (DH) were separated into different fractions with molecular weight cutoff (MWCO) sizes of 10, 3 and 1 kDa, respectively and assayed for ACE inhibitory activity. Skin and bone gelatins had highest DH of 64.87 and 68.48 % after 2 and 1 h incubation, respectively. Results from this study indicated that by decreasing the molecular weight of fractions, ACE inhibitory activity was increased. Therefore, F 3 permeates (MWCO< 1 kDa) of skin (IC 50 03.2 μg/ml) and bone (IC 50 01.3 μg/ml) gelatins possessed higher ACE inhibitory activity compared to their untreated gelatins and corresponding hydrolyzed fractions. In this study, the major amino acids were Glycine followed by Proline with an increased amount of hydrophobic amino acid content in F 3 permeates of skin (4.01 %) and bone (5.79 %) gelatin. Digestion stability against gastrointestinal proteases did not show any remarkable change on ACE inhibition potency of these permeates. It was concluded that alcalase hydrolysis of P. sutchi by-products could be utilized as a part of functional food or ingredients of a formulated drug in order to control high blood pressure.

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“…The apparent K i values were calculated with 31, 32 and 115 lg ml -1 for the 1, 5 and 10 kDa MWCO peptide mixtures, respectively. In comparison, the apparent K i -value for captopril, a competitive pharmaceutical inhibitor for the treatment of hypertension, is reported to be 6.7 ng ml -1 [27]. However, the presence of peptides with different inhibition mechanisms was still possible due to the heterogeneity of the generated peptide mixtures.…”

Section: Antihypertensive Effect and Mechanism Of Ace Inhibitionmentioning

confidence: 99%

“…However, the presence of peptides with different inhibition mechanisms was still possible due to the heterogeneity of the generated peptide mixtures. Typically, the mechanism of ACE inhibition is competitive [28]; however, uncompetitive, non-competitive, competitive as well as mixed inhibition mechanisms have been reported in the literature [27][28][29]. Furthermore, the two peptides V-b-casomorphin-9 (VYPFPGPIPN) and casecidin-17 (YQEPVLGPVRGPF-PIIV) were assayed separately for ACE inhibitory activity.…”

Section: Antihypertensive Effect and Mechanism Of Ace Inhibitionmentioning

confidence: 99%

Bioactive peptides generated in an enzyme membrane reactor using Bacillus lentus alkaline peptidase

Eisele

Stressler

Kranz

et al. 2013

Eur Food Res Technol

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Bacillus lentus alkaline peptidase (BLAP) was used for casein (CN) hydrolysis in an enzyme membrane reactor (EMR) because it was found that BLAP was competitively inhibited by its products. The employed membranes had different molecular weight cut-offs (MWCO 1, 5 and 10 kDa). It was shown that the productivity of the EMR could be significantly improved (28 %) in comparison with batch hydrolysis under the same conditions after 20 h. All resulting EMR peptide mixtures showed a homogenous peptide pattern in HPLC-UV analysis. The obtained peptide mixtures exhibited Angiotensin-I-converting enzyme (ACE) inhibitory and antioxidative activity. The ACE inhibition of the peptide mixtures was dependent on the MWCO of the membranes. The resulting apparent IC 50 values were 115, 131 and 420 lg ml -1 for the 1, 5 and 10 kDa MWCO membranes, respectively. In kinetic studies, a mixed-type inhibition was observed for the three peptide mixtures. The radical scavenging activity was determined with the ABTS assay, and IC 50 values between 20 and 25 lg ml -1 were obtained for the generated peptide mixtures. In addition, the identified VYPFPGPIPN peptide exhibited ACE inhibition and antioxidant activity with IC 50 values of 325 and 6.2 lM, respectively. The peptide YQEPVLGPVRGPFPIIV exhibited radical scavenging activity with an IC 50 value of 5.2 lM.

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ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)

Cited by 135 publications

References 32 publications

Antioxidant and Angiotensin 1 Converting Enzyme Inhibitory Functions from Chicken Collagen Hydrolysates

Antioxidant and Angiotensin 1 Converting Enzyme Inhibitory Functions from Chicken Collagen Hydrolysates

ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

Bioactive peptides generated in an enzyme membrane reactor using Bacillus lentus alkaline peptidase

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