Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Faculty Publications Article Faculty Publications -Articles Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Creator An entity primarily responsible for making the resource Gopalraaj, Jhanani; Velayudhannair, Krishnakumar Title A name given to the resource Kinetic characterisation of proteases from Punica granatum, Musa acuminata, Carica papaya, and Ananas comosus as sustainable enzyme sources Date A point or period of time associated with an event in the lifecycle of the resource 01-01-2026 Source A related resource from which the described resource is derived Biomass Conversion and Biorefinery;Volume;16;Issue;1;Article No.;14; Identifier An unambiguous reference to the resource within a given context <a href="https://doi.org/10.1007/s13399-025-07037-y" target="_blank" rel="noreferrer noopener">https://doi.org/10.1007/s13399-025-07037-y</a> <br /><br /><a href="https://www.scopus.com/pages/publications/105026360855?origin=resultslist" target="_blank" rel="noreferrer noopener">https://www.scopus.com/pages/publications/105026360855?origin=resultslist</a> Coverage The spatial or temporal topic of the resource, the spatial applicability of the resource, or the jurisdiction under which the resource is relevant Gopalraaj J., Department of Life Sciences, Christ University, Hosur Main Road, Dharmaram College Post, Karnataka, Bengaluru, 560 029, India; Velayudhannair K., Department of Life Sciences, Christ University, Hosur Main Road, Dharmaram College Post, Karnataka, Bengaluru, 560 029, India Description An account of the resource Proteases are vital industrial enzymes, contributing approximately 60% of the global enzyme market, by facilitating protein hydrolysis. Fruit peels, a major agricultural waste, offer a sustainable alternative for commercial enzyme production. This study investigates the proteases extracted from the peels of Punica granatum, Musa acuminata, Carica papaya, and Ananas comosus, with a primary focus on determining their optimal pH, temperature, and substrate specificity. Additionally, K? and V??? kinetics were assessed to characterize their catalytic efficiency. Optimal proteolytic activity was observed at pH 8 and 30C for P. granatum, pH 7 and 30C for M. acuminata, pH 8 and 30C for C. papaya, and pH 7 and 50C for A. comosus. substrate specificity of protease was assessed using casein, fish meal, soybean meal, black soldier fly larvae, bovine serum albumin, and egg albumin, revealing broad applicability, especially in P. granatum peels. The stability of P. granatum proteases across substrates suggests multiple isoforms or a flexible active site. Kinetic analysis using Lineweaver-Burk plots revealed Vmax and KM values of 8.45 mol/min/mL and 3.81 M (P. granatum), 4.56 mol/min/mL and 10.08 M (M. acuminata), 2.98 mol/min/mL and 2.84 M (C. papaya), and 2.97 mol/min/mL and 11.38 M (A. comosus) respectively. Among the tested fruit peels, P. granatum exhibited the highest reaction rate, while C. papaya demonstrated the highest substrate affinity, making them as promising candidates for feed supplementation and industrial enzyme applications. The broad substrate specificity and high catalytic efficiency of P. granatum further reinforce its potential for use in feed formulations, enhancing protein hydrolysis and improving nutrient availability. These findings highlight the significant potential of fruit peel-derived proteases in promoting sustainable enzyme production and advancing bioeconomic applications. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2026. Subject The topic of the resource Circular economy; Enzyme kinetics; agro-industrial waste utilisation; Sustainable bioprocessing Publisher An entity responsible for making the resource available Springer Science and Business Media Deutschland GmbH Relation A related resource ISSN: 21906815; Language A language of the resource English Type The nature or genre of the resource Article Rights Information about rights held in and over the resource Restricted Access; Hardcopy may be available in the library Format The file format, physical medium, or dimensions of the resource online