Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology

Extracts of leaves, seeds, roots, and stem from a tropical legume, C. ensiformis, were prepared employing buffers and detergent in aqueous solution. Leaf extracts had the highest protein content and the most pronounced peptidase activity with optimal pH in the neutral to alkaline range. All extracts...

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Main Authors:	Gonçalves, Rayane Natshe, Gozzini Barbosa, Suellen Duarte, da Silva-López, Raquel Elisa
Format:	Online
Language:	English
Published:	Hindawi Publishing Corporation 2016
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5005583/

id	pubmed-5005583
recordtype	oai_dc
spelling	pubmed-50055832016-09-14 Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology Gonçalves, Rayane Natshe Gozzini Barbosa, Suellen Duarte da Silva-López, Raquel Elisa Research Article Extracts of leaves, seeds, roots, and stem from a tropical legume, C. ensiformis, were prepared employing buffers and detergent in aqueous solution. Leaf extracts had the highest protein content and the most pronounced peptidase activity with optimal pH in the neutral to alkaline range. All extracts exhibited peaks of activity at various pH values, suggesting the presence of distinctive classes of proteases. N-α-Tosyl-L-arginine methyl ester hydrolysis was maximal at 30°C to 60°C and peptidase activity from all extracts presented very good thermal stability after 24 h incubation at 70°C. C. ensiformis proteases exhibited molecular masses of about 200–57, 40–37, and 20–15 kDa by SDS-PAGE analysis. These enzymes cleaved hemoglobin, bovine serum albumin, casein, and gelatin at different levels. Serine and metalloproteases are the major proteases in C. ensiformis extracts, modulated by divalent cations, stable at 1% of surfactant Triton X-100 and at different concentrations of the reducing agent β-mercaptoethanol. Thus, C. ensiformis expresses a particular set of proteases in distinctive organs with high activity and stability, making this legume an important source of proteases with biotechnological potential. Hindawi Publishing Corporation 2016 2016-08-17 /pmc/articles/PMC5005583/ /pubmed/27630776 http://dx.doi.org/10.1155/2016/3427098 Text en Copyright © 2016 Rayane Natshe Gonçalves et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Gonçalves, Rayane Natshe Gozzini Barbosa, Suellen Duarte da Silva-López, Raquel Elisa
spellingShingle	Gonçalves, Rayane Natshe Gozzini Barbosa, Suellen Duarte da Silva-López, Raquel Elisa Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology
author_facet	Gonçalves, Rayane Natshe Gozzini Barbosa, Suellen Duarte da Silva-López, Raquel Elisa
author_sort	Gonçalves, Rayane Natshe
title	Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology
title_short	Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology
title_full	Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology
title_fullStr	Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology
title_full_unstemmed	Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology
title_sort	proteases from canavalia ensiformis: active and thermostable enzymes with potential of application in biotechnology
description	Extracts of leaves, seeds, roots, and stem from a tropical legume, C. ensiformis, were prepared employing buffers and detergent in aqueous solution. Leaf extracts had the highest protein content and the most pronounced peptidase activity with optimal pH in the neutral to alkaline range. All extracts exhibited peaks of activity at various pH values, suggesting the presence of distinctive classes of proteases. N-α-Tosyl-L-arginine methyl ester hydrolysis was maximal at 30°C to 60°C and peptidase activity from all extracts presented very good thermal stability after 24 h incubation at 70°C. C. ensiformis proteases exhibited molecular masses of about 200–57, 40–37, and 20–15 kDa by SDS-PAGE analysis. These enzymes cleaved hemoglobin, bovine serum albumin, casein, and gelatin at different levels. Serine and metalloproteases are the major proteases in C. ensiformis extracts, modulated by divalent cations, stable at 1% of surfactant Triton X-100 and at different concentrations of the reducing agent β-mercaptoethanol. Thus, C. ensiformis expresses a particular set of proteases in distinctive organs with high activity and stability, making this legume an important source of proteases with biotechnological potential.
publisher	Hindawi Publishing Corporation
publishDate	2016
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5005583/
_version_	1613639578336362496

Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology

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