Angiotensin I-converting Enzyme (ACE) Inhibitory Activity of Ace Inhibitory Peptides Produced during the Fermentation of Pigeon Pea (Cajanus cajan) Tempe

Pebrianti, Suci Apsari; Cahyanto, Muhammad Nur; Indrati, Retno

doi:10.22146/ifnp.46921

Cited by 3 publications

(6 citation statements)

References 28 publications

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“…However, compared with the finding of Pebrianti et al (2019) on the ACE inhibition of peptide fraction of 48 h-fermented pigeon pea tempe, all of the hydrolyzed pigeon pea tempe peptide fractions in the present study underwent decrement, especially the F3 peptides. This result suggests that the activity of bioactive peptides does not depend on their MW or size.…”

Section: Enzyme Inhibitory Activitycontrasting

confidence: 74%

“…The R. oligosporus used in tempe making produced protease that hydrolyzed the protein of the pigeon pea during fermentation. Pebrianti et al (2019) found that the inhibitory activity of 48 h-fermented pigeon pea tempe is 76.14%. The inhibitory activity of unhydrolyzed tempe was only slightly lower than that of the hydrolyzed tempe.…”

Section: Angiotensin-i-converting Enzyme Inhibitory Activity Of the Peptidementioning

confidence: 98%

“…Pigeon pea tempe was prepared in accordance with the method described by Pebrianti et al (2019). Raw pigeon pea was washed and soaked for 24 h. Then, the pigeon pea was boiled for 20 min.…”

Section: Tempe Preparationmentioning

confidence: 99%

“…Fractionation results showed that the peptide fraction with the largest percentage was < 1 kDa fraction (F1). Pebrianti et al (2019) reported that the peptide compositions of pigeon pea tempe are around 45% for F1 (lowest-MW fraction). The percentage of F1 increased after the hydrolysis of digestive enzymes because of the cleavage of large peptides.…”

Section: Dialysis Fractionationmentioning

confidence: 99%

“…Thus, pigeon pea is a potential source of bioactive peptides. A recent research has shown that pigeon pea (C. cajan) tempe exhibits the highest ACE inhibitory activity after 48 h fermentation, making it a potential functional food to lower hypertension (Pebrianti et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

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Effect of simulated gastrointestinal digestion of bioactive peptide from pigeon pea (Cajanus cajan) tempe on angiotensin-I converting enzyme inhibitory activity

Putra

Marsono

Indrati

2020

NFS

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Purpose The purpose of this paper is to understand the effect of hydrolysis by pepsin and pancreatin on the angiotensin-I-converting enzyme (ACE) inhibitory activity of bioactive peptide from pigeon pea tempe and the absorption of pigeon pea tempe peptide by using the everted gut sac method. Design/methodology/approach The tempe was prepared by inoculating Raprima (Rhizopus oligosporus) on hulled-cooked pigeon pea for 48 h. The extraction was performed using the ultrasonic method at 40 kHz frequency and 100% ultrasonic power for 10 min. The extracted protein was placed in simulated gastrointestinal digestion using consecutive pepsin–pancreatin for 240 min. The hydrolysates were fractionated using a dialysis tube, and its absorption was assessed using the everted Sprague–Dawley rat gut sac. Findings The tempe protein from the hydrolyzed pigeon pea exhibited higher ACE inhibitory (71.53%) activity than that from the boiled pigeon pea (53.04%) (p = 0.028). The bioactive peptide of the digested pigeon pea tempe consisted of low-molecular-weight peptides (<1 kDa). The fraction also showed the highest ACE inhibition activity among the others (IC50 = 0.61 mg/mL, p = 0.021). Bioactive peptides from pigeon pea tempe were absorbed well in the small intestine, mainly in the jejunum. The activity of the absorbed peptides did not change considerably. Originality/value The activity of bioactive peptide of pigeon pea tempe was comparatively stable during digestion. It exhibited activity even after absorption in the small intestine. Thus, pigeon pea tempe can serve as an antihypertensive peptide source and alternative food for maintaining/reducing blood pressure.

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Section: Enzyme Inhibitory Activitycontrasting

confidence: 74%

Section: Angiotensin-i-converting Enzyme Inhibitory Activity Of the Peptidementioning

confidence: 98%

“…Pigeon pea tempe was prepared in accordance with the method described by Pebrianti et al (2019). Raw pigeon pea was washed and soaked for 24 h. Then, the pigeon pea was boiled for 20 min.…”

Section: Tempe Preparationmentioning

confidence: 99%

Section: Dialysis Fractionationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Effect of simulated gastrointestinal digestion of bioactive peptide from pigeon pea (Cajanus cajan) tempe on angiotensin-I converting enzyme inhibitory activity

Putra

Marsono

Indrati

2020

NFS

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Low molecular weight peptides generated from palm kernel cake via solid state lacto-fermentation extend the shelf life of bread

Asri

Muhialdin

Zarei

et al. 2020

LWT

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This study aimed at investigating the potential antifungal activity of low molecular weight peptides being a natural preservative generated from palm kernel cake (PKC) via solid state lacto-fermentation. Palm kernel cake was hydrolysed by L. casei generating a peptide mixture with a DH of 43.39% under predetermined optimum conditions of 5.6 days incubation, 3% glucose, and substrate/water ratio of 48/52 w/v. A total of 10 cationic peptides with molecular weight ranging from 932 to 1869 Da were identified by LC/MS-MS, in which 7 belonged to oil palm proteins and 3 de novo peptides biosynthesized by the microorganism during the fermentation process. The aqueous extract of the peptides mixture demonstrated strong antifungal activity against Aspergillus flavus (69.15%), Aspergillus niger (88.08%), Fusarium sp. (87.14%), and Penicillium sp. (71.84%). 1H-NMR spectroscopy results showed the presence of trace amounts of lactic and acetic acid, indicating that the antimicrobial activity was solely attributed by the low molecular weight peptides. The peptides mixture successfully delayed fungal growth, thus extending the shelf life of bread for up to 10 days when added to the bread at 2000 mg/kg. These findings indicated a promising application of the peptides mixture as a bio-preservative in extending the shelf life of bread.

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Effect of legume varieties and fermentation time of tempe using usar inoculum on the inhibitory activity of angiotensin I-converting enzyme

Indrati¹,

Handayani²,

Rahayu³

et al. 2021

Biodiversitas

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Abstract. Indrati R, Handayani MT, Rahayu NA, Pebrianti SA. 2021. Effect of legume varieties and fermentation time of tempe using usar inoculum on the inhibitory activity of angiotensin I-converting enzyme. Biodiversitas 22: 5262-5267. The effect of three varieties of legumes, namely, velvet bean (Mucuna prurient), lima bean (Phasaelus lunatus L.), and pigeon pea (Cajanus cajan), on the activity of angiotensin I-converting enzyme (ACE) inhibitors was studied during tempe fermentation. Fermentation is one way to produce bioactive peptides. Furthermore, the effect of inoculum usar on tempe fermentation was studied. Hydrophobic amino acids are essential in binding firmly to the active site of ACE, and the research showed that pigeon pea had higher levels of hydrophobic amino acids compared with soybeans. The legumes affected the protease activity, peptide content, degree of hydrolysis, and production of ACE inhibitory (ACEI) activity during tempe fermentation. High protein levels and peptide content did not guarantee a high ACE inhibitor level. The mixed culture of usar caused no effect on the production of ACE inhibitors compared with a single culture of Raprima. Legume beans that reached optimal fermentation fast produced high levels of ACE inhibitors. Of the three types of legumes tested in the study, lima beans had the highest ACEI activity during fermentation.

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Angiotensin I-converting Enzyme (ACE) Inhibitory Activity of Ace Inhibitory Peptides Produced during the Fermentation of Pigeon Pea (Cajanus cajan) Tempe

Cited by 3 publications

References 28 publications

Effect of simulated gastrointestinal digestion of bioactive peptide from pigeon pea (Cajanus cajan) tempe on angiotensin-I converting enzyme inhibitory activity

Effect of simulated gastrointestinal digestion of bioactive peptide from pigeon pea (Cajanus cajan) tempe on angiotensin-I converting enzyme inhibitory activity

Low molecular weight peptides generated from palm kernel cake via solid state lacto-fermentation extend the shelf life of bread

Effect of legume varieties and fermentation time of tempe using usar inoculum on the inhibitory activity of angiotensin I-converting enzyme

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