There is an ever-increasing demand for industrial enzyme, necessitating a constant search for its efficient producers. The isolation and characterization of invertase producer yeasts from natural palm wine is reported in this study. Yeasts were isolated from fresh palm wine obtained from Abagboro community Ile-Ife, Nigeria following standard methods. A total of six yeast strains were isolated from the palm wine. The strains were screened for their ability to produce invertase and the most efficient invertase producer was characterized and identified using phenotypic and molecular methods. Isolate C showed the highest invertase activity (34.15 µmole/ml/min), followed by isolate B (18.070 µmole/ml/min) and isolate A (14.385 µmole/ml/min). The identity of isolate C was confirmed by genotypic methods to be Saccharomyces cerevisiae (OL629078.1 accession number on NCBI database). The Saccharomyces cerevisiae strain fermented galactose, arabinose, maltose, glucose, sucrose and raffinose, grew in 50% and 60% glucose and at 25–35 °C. The newly isolated Saccharomyces cerevisiae strain is an efficient producer of invertase and can be exploited for commercial biosynthesis of the enzyme for use in biotechnological applications.
The ability of yeast to secrete intracellular and extracellular forms of invertase has been demonstrated by studies, however not much research has focused on intracellular invertase. Here we report the biochemical and chromatographic properties of intracellular invertase from invertase hyperproducer obtained from Abagboro village, Ile-Ife, Nigeria and compared it with that from a brewery which had been commercially selected. Saccharomyces cerevisiae and Saccharomyces carlsbergensis were isolated from fresh palm wine obtained from Abagboro village, Ile-Ife and from green beer obtained from a local brewery, respectively. Isolates were grown on liquefied cassava-soy bean mash for 72 hours. Yeast biomass harvested was homogenized to obtain crude intracellular invertase and purified by chromatographic techniques. Physicochemical properties and kinetic parameters (Km and Vmax) of the enzymes was studied. Native and subunit molecular weights of purified invertase from an hyperproducer (Saccharomyces cerevisiae) and brewer’s yeast (Saccharomyces carlsbergensis) were 118.3 kDa and 113.38 ± 4.9 kDa; 39.12 ± 1.2 kDa and 39.34 ± 1.71 kDa, respectively. Invertase was stable for 1 hour at 50 oC, with optimum temperature of 50 oC and 55 oC for Saccharomyces cerevisiae and Saccharomyces carlsbergensis, while their activation energies were 36.225 ± 4.015 kJmol− 1 and 33.06 ± 1.810 kJmol− 1 respectively. Invertase from Saccharomyces cerevisiae and Saccharomyces carlsbergensis had optimum activity at pH 5.0 and 4.0 respectively. Both enzymes utilized similar substrates with highest affinities for sucrose. The newly identified intracellular invertase from Abagboro yeast share similar physicochemical properties with that from commercial yeast (Saccharomyces carlsbergensis).
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.