Post-proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications

Baharin, Anis; Ting, Tiew-Yik; Goh, Hoe-Han

doi:10.20944/preprints202204.0097.v1

Cited by 2 publications

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“…There is a serine protease named prolyl oligopeptidase (POP) that has the potential to degrade peptide hormones and proline‐containing neuropeptides, with implications for aging and neurodegeneration (Baharin, Ting, & Goh, 2022). The potential of the SPH and peptide fractions to inhibit the POP enzyme was estimated by determining IC 50 values (Table 2).…”

Section: Resultsmentioning

confidence: 99%

Antioxidant and enzyme inhibitory properties of sacha inchi ( Plukenetia volubilis ) protein hydrolysate and its peptide fractions

Suwanangul

Aluko

Sangsawad

et al. 2022

Journal of Food Biochemistry

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The objective of this study was to determine the in vitro activities such as antioxidant and inhibitions of angiotensin converting enzyme, dipeptidyl peptidase‐IV, prolyl oligopeptidase, and 3‐hydroxy‐3‐methyl‐glutaryl‐coenzyme A reductase of sacha inchi protein hydrolysate (SPH) and its membrane ultrafiltration peptide fractions. SPH was prepared after hydrolysis of sacha inchi protein using papain followed by separation into peptide fractions (F1: <1 kDa, F2: 1–3 kDa, F3: 3–5 kDa, and F4: 5–10 kDa) via ultrafiltration membranes. SPH and the peptide fractions were tested for multifunctional properties, specifically functional ability as antioxidants and enzyme inhibitors. Surface hydrophobicity was an important contributing factor to the activity of antioxidative peptides. The DPPH inhibitory activity of F4 was significantly higher (p < .05) than activities of the SPH and other fractions. The smaller peptides with <1 kDa size (F1) showed the most potent (p < .05) antioxidant properties based on the stronger scavenging of ABTS, DPPH, and superoxide radicals in addition to better attenuation of linoleic acid peroxidation. Moreover, the F1 was also the strongest inhibitor of angiotensin converting enzyme, dipeptidyl peptidase‐IV, prolyl oligopeptidase inhibition, and 3‐hydroxy‐3‐methyl‐glutaryl‐coenzyme A reductase based on the lower IC50 values. It was concluded that the smaller size of the F1 peptides was the main determinant of its strong antioxidant and enzyme inhibition potency, which could be taken as an advantage to formulate functional foods and nutraceuticals with potential activities in ameliorating some of the chronic human diseases. Practical applications The results of present study indicate that SPH and its ultrafiltration fractions are potential sources of antihypertensive, antidiabetic, inhibition of POP, reduced cholesterol, and strong antioxidant peptides. The strong angiotensin converting enzyme, dipeptidyl peptidase‐IV, prolyl oligopeptidase inhibition, and 3‐hydroxy‐3‐methyl‐glutaryl‐coenzyme inhibitory efficiency of the F1 peptides (MW < 1 kDa) suggest potential utility as an antihypertensive, antidiabetic agent, reduce cholesterol and brain plasticity and memory formation because the small peptide size could enhance absorption from the gastrointestinal tract. Overall, results from this study indicate that SPH, especially the F1 peptides may have applications as ingredients for the formulation of functional foods and nutraceuticals.

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Section: Resultsmentioning

confidence: 99%

Antioxidant and enzyme inhibitory properties of sacha inchi ( Plukenetia volubilis ) protein hydrolysate and its peptide fractions

Suwanangul

Aluko

Sangsawad

et al. 2022

Journal of Food Biochemistry

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The Complex World of Emaraviruses—Challenges, Insights, and Prospects

Rehanek

Karlin

Bandte

et al. 2022

Forests

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Emaravirus (Order Bunyavirales; Family Fimoviridae) is a genus comprising over 20 emerging plant viruses with a worldwide distribution and economic impact. Emaraviruses infect a variety of host plants and have especially become prevalent in important long-living woody plants. These viruses are enveloped, with a segmented, single-stranded, negative-sense RNA genome and are transmitted by eriophyid mites or mechanical transmission. Emaraviruses have four core genome segments encoding an RNA-dependent RNA polymerase, a glycoprotein precursor, a nucleocapsid protein, and a movement protein. They also have additional genome segments, whose number varies widely. We report here that the proteins encoded by these segments form three main homology groups: a homolog of the sadwavirus Glu2 Pro glutamic protease; a protein involved in pathogenicity, which we named “ABC”; and a protein of unknown function, which we named “P55”. The distribution of these proteins parallels the emaravirus phylogeny and suggests, with other analyses, that emaraviruses should be split into at least two genera. Reliable diagnosis systems are urgently needed to detect emaraviruses, assess their economic and ecological importance, and take appropriate measures to prevent their spread (such as routine testing, hygiene measures, and control of mite vectors). Additional research needs include understanding the function of emaravirus proteins, breeding resistant plants, and clarifying transmission modes.

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Post-proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications

Cited by 2 publications

References 0 publications

Antioxidant and enzyme inhibitory properties of sacha inchi ( Plukenetia volubilis ) protein hydrolysate and its peptide fractions

Antioxidant and enzyme inhibitory properties of sacha inchi ( Plukenetia volubilis ) protein hydrolysate and its peptide fractions

The Complex World of Emaraviruses—Challenges, Insights, and Prospects

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