Angiotensin‐converting enzyme inhibitory and antioxidant peptides from digestion of larvae and pupae of Asian weaver ant, <i>Oecophylla smaragdina</i>, Fabricius

Pattarayingsakul, Werawich; Nilavongse, Arjaree; Reamtong, Onrapak; Chittavanich, Pamorn; Mungsantisuk, Idsada; Mathong, Yuvadee; Prasitwuttisak, Wipoo; Panbangred, Watanalai

doi:10.1002/jsfa.8155

Cited by 31 publications

(29 citation statements)

References 35 publications

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“…BLPHs‐I had lowest 50% inhibition concentration (IC 50 ) (0.76 mg/ml), indicating the higher scavenging activity ( p < .05) than that of BLPHs (IC 50 = 0.85 mg/ml), BLPHs‐II (IC 50 = 1.27 mg/ml), and BLPHs‐III (IC 50 = 1.21 mg/ml). This result is consistent with previous results (Pattarayingsakul et al, 2017) who reported that low molecular components from Asian weaver ant ( O. smaragdina ) protein hydrolysates also possessed good scavenging activity. Male silkmoth protein hydrolysate with MW <3 kDa exhibited higher DPPH scavenging activity (Liu et al, 2017).…”

Section: Resultssupporting

confidence: 93%

“…The commercial enzymes are used to promote the hydrolysis of protein improve its bioactivity by converting it into peptides while retaining its nutritive value (Moure, Domínguez, & Parajó, 2006). Numerous studies over the recent years have demonstrated the antioxidant properties of hydrolyzed proteins from multiple insects species, such as weaver ant ( Oecophylla smaragdina ) (Pattarayingsakul et al, 2017), male silkmoth (Liu, Wan, Liu, Zou, & Liao, 2017), and queen bee (Dong, Dong, Liu, Lu, & Yu, 2017). However, studies on the antioxidant activity of the BLP hydrolysates (BLPHs) are rarely reported, and few antioxidant sequences of BSF have been reported before.…”

Section: Introductionmentioning

confidence: 99%

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Preparation, antioxidant activity evaluation, and identification of antioxidant peptide from black soldier fly ( Hermetia illucens L.) larvae

Ding

Huang

et al. 2020

J Food Biochem

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Black soldier fly larvae protein (BLP) was hydrolyzed using alcalase, neutrase, trypsin, and papain. The BLP hydrolysates (BLPHs) were fractionated by ultrafiltration into three peptide fractions of molecular weight (<3 kDa, 3–10 kDa and >10 kDa). Their antioxidant activities in vitro and the amino acid composition were determined. Results showed that the alcalase was more efficient in hydrolyzing the BLP into oligopeptides. BLPHs‐I presented the best scavenging activity to superoxide radicals, hydroxyl radicals, DPPH, and ABTS radicals. The best scavenging activities were found in BLPHs‐I containing high levels of aromatic and hydrophobic amino acids. Seventeen novel sequences with typical features of well‐known antioxidant proteins were identified by LC‐MS/MS. Results demonstrated that BLPHs‐I possesses a great capacity as antioxidant peptides applied in functional foods. Practical applications Black soldier fly larvae protein (BLP) can also be hydrolyzed to produce antioxidant peptides and their sequences were identified. It can be used in pharmaceutical products and functional foods.

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Section: Resultssupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Preparation, antioxidant activity evaluation, and identification of antioxidant peptide from black soldier fly ( Hermetia illucens L.) larvae

Ding

Huang

et al. 2020

J Food Biochem

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“…They contain more than 50% crude protein, according to a nutritional value evaluation, and contain more than 20 amino acids; various microelements; special chemicals, such as formic acid and herbaceous acetaldehyde, which are triterpenoid compounds, and several vitamins (Pattarayingsakul et al, 2017). Many pangolin genes are likely to be involved in the digestion of these materials because 27 of the transcripts related to the terpenoid backbone biosynthesis, and this might be one of the biological basis for their adaptions to myrmecophagy.…”

Section: Discussionmentioning

confidence: 99%

Transcriptomic analysis identifies genes and pathways related to myrmecophagy in the Malayan pangolin (Manis javanica)

Ma¹,

Li²,

Jiang³

et al. 2017

PeerJ

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The Malayan pangolin (Manis javanica) is an unusual, scale-covered, toothless mammal that specializes in myrmecophagy. Due to their threatened status and continuing decline in the wild, concerted efforts have been made to conserve and rescue this species in captivity in China. Maintaining this species in captivity is a significant challenge, partly because little is known of the molecular mechanisms of its digestive system. Here, the first large-scale sequencing analyses of the salivary gland, liver and small intestine transcriptomes of an adult M. javanica genome were performed, and the results were compared with published liver transcriptome profiles for a pregnant M. javanica female. A total of 24,452 transcripts were obtained, among which 22,538 were annotated on the basis of seven databases. In addition, 3,373 new genes were predicted, of which 1,459 were annotated. Several pathways were found to be involved in myrmecophagy, including olfactory transduction, amino sugar and nucleotide sugar metabolism, lipid metabolism, and terpenoid and polyketide metabolism pathways. Many of the annotated transcripts were involved in digestive functions: 997 transcripts were related to sensory perception, 129 were related to digestive enzyme gene families, and 199 were related to molecular transporters. One transcript for an acidic mammalian chitinase was found in the annotated data, and this might be closely related to the unique digestive function of pangolins. These pathways and transcripts are involved in specialization processes related to myrmecophagy (a form of insectivory) and carbohydrate, protein and lipid digestive pathways, probably reflecting adaptations to myrmecophagy. Our study is the first to investigate the molecular mechanisms underlying myrmecophagy in M. javanica, and we hope that our results may play a role in the conservation of this species.

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“…The protein solution was centrifuged at 3000 g for 10 min at 4°C to collect soluble proteins in supernatant, and non-soluble materials were discarded. The digestion of proteins using pepsin (≥250 units mg −1 ) and trypsin (1000-2000 BAEE units mg −1 ) was performed as described in Pattarayingsakul et al (2017). Briefly, protein solution was adjusted to pH 2 using 6 M HCl and was digested using pepsin (0.4% w/v), at 37°C for 2 h. The pH of protein hydrolysates was then adjusted to 7.5 using 1 M NaHCO 3 and further digested at 37°C for another 2 h using trypsin (0.4% w/v).…”

Section: Preparation Of Protein Hydrolysates and Protein Fractionationmentioning

confidence: 99%

In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins

Aiemratchanee

Panyawechamontri

Phaophu

et al. 2020

Int J of Food Sci Tech

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New bioactive peptides with antihypertensive property from red blood corpuscle (RBC) and plasma (PL) hydrolysate fractions of porcine blood were identified. Three peptides with the highest Angiotensin-converting enzyme (ACE) inhibitory activity from RBC, including RBC7 (TPYPCV), RBC15 (VVYPWR) and RBC9 (FLCT), showed IC 50 values of 2.58 AE 0.87, 5.22 AE 2.56 and 6.53 AE 0.34 µM, respectively. By comparison, PL1 (YTFPFH), PL2 (WGHGNPHV) and PL7 (VPLW) from PL displayed higher IC 50 values at 24.12 AE 2.44, 15.33 AE 0.44 and 32.80 AE 38.96 µM, respectively. Molecular docking was employed to simulate the interactions of RBC7 and RBC15 with the catalytic site of the ACE receptor. RBC7 and RBC15 interacted with residues in the ACE receptor that normally coordinated with Zn(II), and RBC7 also interacted extensively with residues within S1, S2 and S'1 active sites. Taken together, these results illustrate that porcine blood is an excellent source of antihypertensive peptides and could be of great benefits to people with high blood pressure.

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Angiotensin‐converting enzyme inhibitory and antioxidant peptides from digestion of larvae and pupae of Asian weaver ant, Oecophylla smaragdina, Fabricius

Abstract: These results indicate that proteins from larvae and pupae of weaver ants are potential sources of peptides with anti-ACE and antioxidation bioactivities. © 2016 Society of Chemical Industry.

Cited by 31 publications

References 35 publications

Preparation, antioxidant activity evaluation, and identification of antioxidant peptide from black soldier fly ( Hermetia illucens L.) larvae

Preparation, antioxidant activity evaluation, and identification of antioxidant peptide from black soldier fly ( Hermetia illucens L.) larvae

Transcriptomic analysis identifies genes and pathways related to myrmecophagy in the Malayan pangolin (Manis javanica)

In vitro antihypertensive activity of bioactive peptides derived from porcine blood corpuscle and plasma proteins

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