Isolation and Antihypertensive Effect of Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Spinach Rubisco

Yang, Yongjian; Marczak, Ewa D.; Yokoo, Megumi; Usui, Hachiro; Yoshikawa, Masaaki

doi:10.1021/jf026186y

Cited by 115 publications

(79 citation statements)

References 23 publications

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“…The hydrolysis with the sequential pepsinpancreatin system was done for 90 min: predigestion with pepsin for 45 min followed by incubation with pancreatin for 45 min. Hydrolysis parameters were substrate concentration 4%; enzyme/substrate ratio 1:10; pH 2.0 for pepsin; pH 7.5 for pancreatin; and 378C hydrolysis temperature (Megı´as et al, 2004;Yang, Marczak, Yokoo, Usui, & Yoshikawa, 2003). In both treatments, the reaction was stopped by heating to 808C for 20 min, followed by centrifuging at 1317 x g for 12 min (Mistral 3000i, Curtin Matheson Sci.)…”

Section: Enzymatic Hydrolysismentioning

confidence: 99%

Antioxidant activity ofVigna unguiculataL. walp and hard-to-cookPhaseolus vulgarisL. protein hydrolysates

Campos

Ruíz-Ruíz

Chel‐Guerrero

et al. 2013

CyTA - Journal of Food

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Recent research, using model systems, has shown that enzymatic hydrolysis of food proteins can make them act as direct scavengers of diverse free radicals. This study aimed at the characterization of protein hydrolysates with antioxidant properties from Vigna unguiculata L. walp and hard-to-cook Phaseolus vulgaris L. protein concentrates. The maximum values obtained for all the assays were 15.1 mM/mg of protein for Trolox-equivalent-antioxidative capacity, 98.2% for percentage of 2,2-diphenyl-1-picrylhydrazyl (DPPH) discoloration, 70.1% and 71.4% for iron and copper chelating activities, respectively. The reducing power of hydrolysates was higher than butylated hydroxytoluene (BHT) (control). The antioxidant activity of the hydrolysates may be a result of enzymatic hydrolysis generating peptides that exhibit this type of activity. The hydrolysates showed an increase of amino acids that have been associated with the biological activity of peptides with antioxidant activity, such as hydrophobic residues: Ala, Phe and Ile; hydrophilic: Lys and neutral: Ser and Gly.Keywords: Vigna unguiculata; Phaseolus vulgaris; hydrolysates; antioxidant activity Estudios recientes han demostrado que los hidrolizados enzima´ticos de proteı´nas alimentarias pueden actuar directamente sobre radicales libres. El objetivo del presente trabajo fue caracterizar las propiedades antioxidantes de hidrolizados proteı´nicos de Vigna unguiculata L. walp y Phaseolus vulgaris L. endurecido. Los valores ma´ximos obtenidos para las determinaciones efectuadas fueron, 15,1 mM/mg de proteı´na de Capacidad Antioxidante Equivalente de Trolox, 98,2% de decoloracio´n del radical DPPH, 70,1% y 70,4% de capacidad quelante de cobre y hierro, respectivamente. El poder reductor de los hidrolizados fue superior al del BHT (control). La capacidad antioxidante posiblemente se relacione conlos pe´ptidos generados durante la hidrolisis, los cuales presentan dicha actividad. La composicio´n aminoacı´dica de los hidrolizados mostro´un incremento de aminoa´cidos hidrofo´bicos (Ala, Fen e Ile), hidrofı´licos (Lis) y neutros (Ser y Gli), los cuales han sido asociados a la secuencia de pe´ptidos con actividad antioxidantes.

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Section: Enzymatic Hydrolysismentioning

confidence: 99%

Antioxidant activity ofVigna unguiculataL. walp and hard-to-cookPhaseolus vulgarisL. protein hydrolysates

Campos

Ruíz-Ruíz

Chel‐Guerrero

et al. 2013

CyTA - Journal of Food

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“…It is secreted in the lungs and kidneys by cells in the endothelium of blood vessels (Kierszenbaum, 2007). ACE inhibiting four different peptides MRWRD, MRW, LRIPVA, and IAYKPAG were isolated from spinach RuBisCO (Yang et al, 2003). High frequency of occurance of ACE inhibiting peptides in microalgal and cyanobacterial RuBisCo sequences provide a promising platform for sustainable production of potent ACE inhibiory peptide based anti-hypersenstive drugs.…”

Section: Physio-chemical Parameters Of the Selected Sequencesmentioning

confidence: 99%

Computational screening of microalgae and cyanobacteria RuBisCO as potential precursor for bioactive peptides

Selvaraj

Kaliamurthi

Çakmak

et al. 2017

Preprint

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Ribulose-1,5-bisphosphate carboxylase/oxygense (RuBisCO) is present in plants and autotrophic organisms like microalgae. The aim of this study was to perform an in silico evaluation of RuBisCo protein in microalgae and cyanobacteria as potential precursors of bioactive peptides, as well as to determine whether such peptides can be released by selected proteolytic enzymes. Fourteen RuBioCo sequences of microalgae and cyanobacteria were analysed by using the BIOPEP server amd database. The biological activity, enzyme action and calculation of active peptide tools were used to determine the frequency of occurrence of fragments, proteolysis, and the frequency of release of fragments with given activity by Dunaliella salina, Chlorella pyrenoidosa, and Chlorella vulgaris are associated with a high content of glycine and proline amino acids that are most rich in biologically active fragments.

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“…Accordingly, if peptides capable of acting as a substrate for ACE exist in food-derived protein hydrolyzates, it follows that these hydrolyzates will exhibit ACE inhibitory activity. Moreover, there are some reports that the actual hypotensive effect of peptides, which were isolated from protein hydrolyzates showing ACE inhibitory activity, was induced by other hypotensive mechanisms, such as vasorelaxation, besides ACE inhibitory activity (Yang et al, 2003;Zhao et al, 2008;Yamada et al, 2010). Therefore, the elucidation of other mechanisms regulating the hypotensive effect of YRLP in SHR is a subject of future research.…”

Section: Fig 1 Hplc Chromatogram Of Peptides In the S2 Fraction Shmentioning

confidence: 99%

Angiotensin-Converting Enzyme-Inhibitory Peptides Isolated from Pepsin Hydrolyzate of Apios americana Tuber and Their Hypotensive Effects in Spontaneously Hypertensive Rats

Kuramoto

Kaneyoshi

Morinaga

et al. 2013

FSTR

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With the aim of elucidating the hypotensive effects of Apios americana Medikus tuber, active ingredients with angiotensin-converting enzyme (ACE)-inhibitory activity were identified and their hypotensive effects in spontaneously hypertensive rats (SHR) were investigated. From a pepsin digest of A. americana showing strong activity, two ACE-inhibitory peptides were isolated and identified as YRLPNL and YQLP. Although the ACE-inhibitory activity of YQLP was weak, YRLPNL showed strong ACE-inhibitory activity (IC 50 value 7.7 nM) equal to those of lisinopril and captopril. After a single oral administration of YRLPNL, SHR showed a significant decrease in blood pressure. These results suggest that YRLPNL, isolated from A. Americana, is a hypotensive peptide having ACE-inhibitory activity. This is the first report of a food peptide having ACE-inhibitory activity equal to that of pharmaceuticals.

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Isolation and Antihypertensive Effect of Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Spinach Rubisco

Cited by 115 publications

References 23 publications

Antioxidant activity ofVigna unguiculataL. walp and hard-to-cookPhaseolus vulgarisL. protein hydrolysates

Antioxidant activity ofVigna unguiculataL. walp and hard-to-cookPhaseolus vulgarisL. protein hydrolysates

Computational screening of microalgae and cyanobacteria RuBisCO as potential precursor for bioactive peptides

Angiotensin-Converting Enzyme-Inhibitory Peptides Isolated from Pepsin Hydrolyzate of Apios americana Tuber and Their Hypotensive Effects in Spontaneously Hypertensive Rats

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