Isolation, Characterization, and Biocompatibility of Bisporitin, a Ribotoxin-like Protein from White Button Mushroom ( Agaricus bisporus ).

Autor: Ragucci S; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Hussain HZF; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Bosso A; Department of Biology, University of Naples 'Federico II', Via Cinthia 26, 80126 Naples, Italy., Landi N; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Clemente A; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Pedone PV; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy., Pizzo E; Department of Biology, University of Naples 'Federico II', Via Cinthia 26, 80126 Naples, Italy.; Centro Servizi Metrologici e Tecnologici Avanzati (CeSMA), University of Naples 'Federico II', 80126 Naples, Italy., Di Maro A; Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, 81100 Caserta, Italy.
Jazyk: angličtina
Zdroj: Biomolecules [Biomolecules] 2023 Jan 26; Vol. 13 (2). Date of Electronic Publication: 2023 Jan 26.
DOI: 10.3390/biom13020237
Abstrakt: White button mushroom ( Agaricus bisporus (J.E. Lange) Imbach) is one of the widely consumed edible mushrooms. Indeed, A. bisporus fruiting bodies are a rich source of nutrients and bioactive molecules. In addition, several enzymes with biotechnological applications are found in A. bisporus (e.g., enzymes for lignocellulose degradation). Here, a novel ribotoxin-like protein (RL-P) from the edible mushroom A. bisporus was purified and characterized. This RL-P, named bisporitin, is a monomeric protein (17-kDa) exhibiting specific ribonucleolytic activity by releasing the α-fragment (hallmark of RL-Ps) when incubated with rabbit ribosomes. In addition, bisporitin shows magnesium-dependent endonuclease activity and displays a similar far-UV CD spectrum as ageritin, the prototype of RL-Ps, isolated from Cyclocybe aegerita fruiting bodies. Interestingly, bisporitin is the first member of RL-Ps to have noticeably lower thermal stability (T m = 48.59 ± 0.98 °C) compared to RL-Ps isolated in other mushrooms (T m > 70 °C). Finally, this protein is only partially hydrolyzed in an in vitro digestive system and does not produce adverse growing effects on eukaryotic cell lines. This evidence paves the way for future investigations on possible bioactivities of this RL-P in the digestive system.
Competing Interests: The authors declare no conflict of interest.
Databáze: MEDLINE
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