The secondary structure of legume (Phaseolus vulgaris L. and Lens culinaris L.) proteins was investigated by studying the amide I infrared absorption band in whole seed flours, before and after dry heating and autoclaving thermal treatments. The analysis procedure, set up on 7S and different model proteins, shows that the content of beta-sheet structures in lentil is higher than in common bean (47% vs. 32%). The dry heating does not appreciably affect secondary structures in lentil, while it causes a reduction of beta-sheets (to 13%), an increase of aggregates, and the appearance of random coil structures in common bean. The autoclaving treatment produces high amounts of aggregates in both legumes. However, in lentil, random coil structures are lower than in common bean and some beta-sheet structures are still detectable. These results indicate that multimeric heat-induced complexes of legume proteins have a high stability because of the high content in beta-sheet structures, in particular in lentil, which may adversely affect protein utilization. (C) 2007 Elsevier Ltd. All rights reserved.
Application of Fourier transform infrared spectroscopy to legume seed flour analysis
Maselli P;Dore P;Nucara A
2008
Abstract
The secondary structure of legume (Phaseolus vulgaris L. and Lens culinaris L.) proteins was investigated by studying the amide I infrared absorption band in whole seed flours, before and after dry heating and autoclaving thermal treatments. The analysis procedure, set up on 7S and different model proteins, shows that the content of beta-sheet structures in lentil is higher than in common bean (47% vs. 32%). The dry heating does not appreciably affect secondary structures in lentil, while it causes a reduction of beta-sheets (to 13%), an increase of aggregates, and the appearance of random coil structures in common bean. The autoclaving treatment produces high amounts of aggregates in both legumes. However, in lentil, random coil structures are lower than in common bean and some beta-sheet structures are still detectable. These results indicate that multimeric heat-induced complexes of legume proteins have a high stability because of the high content in beta-sheet structures, in particular in lentil, which may adversely affect protein utilization. (C) 2007 Elsevier Ltd. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
