FEBS LettersVolume 67, Issue 2 p. 202-206 Full-length articleFree Access Interaction of Tenebrio molitor L. α-amylase with a wheat flour protein inhibitor V. Buonocore, V. Buonocore Istituto di Chimica Organica, Università di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy Laboratori di Chimica Biologica, Istituto Superiore di Sanità, 00136 Roma, ItalySearch for more papers by this authorE. Poerio, E. Poerio Istituto di Chimica Organica, Università di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy Laboratori di Chimica Biologica, Istituto Superiore di Sanità, 00136 Roma, ItalySearch for more papers by this author V. Buonocore, V. Buonocore Istituto di Chimica Organica, Università di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy Laboratori di Chimica Biologica, Istituto Superiore di Sanità, 00136 Roma, ItalySearch for more papers by this authorE. Poerio, E. Poerio Istituto di Chimica Organica, Università di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy Laboratori di Chimica Biologica, Istituto Superiore di Sanità, 00136 Roma, ItalySearch for more papers by this author First published: August 15, 1976 https://doi.org/10.1016/0014-5793(76)80366-3Citations: 20AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume67, Issue2August 15, 1976Pages 202-206 ReferencesRelatedInformation

AbstractElectrophoretic patterns of protein extracts obtained with different procedures from the BP‐yeast product named Toprina (a Candida lipolytica strain grown on n‐alkanes) have been compared with protein electrophoretic patterns of a number of different microbial species. The gel electrophoretic pattern of the 0.15 M NaCl extract from Toprina was specific enough to allow an easy differentiation of Toprina from the other microorganisms tested.To detect and assay Toprina in blends with animal feeds, an immune serum containing antibodies reacting specifically with Toprina has been prepared by immunising rabbits with an antigen preparation extracted from Toprina with 0.15 M NaCl and precipitated by salting out the extract at 4.0 M (NH4)2SO4. Three main antibodies reacting with Toprina antigens have been found in the anti‐Toprina immune serum, but only one was specific of Toprina. The resistance of the Toprina antigens to peptic digestion and their behaviour on extraction, electrophoresis and gel filtration suggest that they might be acidic polysaccharide in nature.Immunodiffusion analyses with the anti‐Toprina immune serum of extracts obtained with 0.15 M NaCl from very heterogeneous animal feeds added with different amounts of Toprina, allowed the detection of a Toprina amount as low as 2.5%. An accurate assay of Toprina was achieved by submitting the feed extract to radial immunodiffusion with the anti‐Toprina immune serum.