ArticleMolecular biology reports2025
Molecular characterization and protein purification of α-galactosidase from penicillium citrinum M(A79) for its industrial applications.
Article in Molecular biology reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundProtein purification is an essential step for complete characterization of any industrially important enzymes isolated from micro-organisms. In the present study, we have successfully isolated and identified fungal strain, Penicillium sp. (AL-3) for the bulk production of α-galactosidase enzyme which shows close phylogenetic resemblance with Penicillium citrinum (A79) using ITS sequencing (5.8 S rRNA and 28 S rRNA gene). METHODS AND
resultsSelected fungus screened for its efficiency for α-galactosidase production using (1% w/v) soybean meal as a carbon substrate in culture media for maximum enzyme secretion. Enzyme was purified using ammonium sulphate precipitation (25-75%) with maximum enzyme activity of 2867.00 U/ml (yield of 90%). The eluted protein was further purified by DEAE ion exchange chromatography with an enzyme activity of 2260.04 U/mL (yield of 70.95%). The estimated molecular weight of the partially-purified enzyme was found to be 33 kDa, using size exclusion chromatography and 81 kDa using SDS-PAGE analysis which reflects its dimeric nature. Enzyme was inhibited by silver (Ag
conclusionPenicillium citrinum strain (A79) showed a high potential for the bulk production of the alpha-galactosidase with enzyme activity reported to be 733-745.15 U/ml under optimized culture conditions. Its properties make it widely applicable for digestive enzyme preparations, food, feed and medical industries.
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