Application of Fourier transform infrared spectroscopy to legume seed flour analysis

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 β-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 β-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 β-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 β-sheet structures, in particular in lentil, which may adversely affect protein utilization.

[1]  S. Damodaran,et al.  Structure‐Digestibility Relationship of Legume 7S Proteins , 1989 .

[2]  Taro Masuda,et al.  Crystal structure of soybean 11S globulin: Glycinin A3B4 homohexamer , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[3]  D. Boulter,et al.  Legumin and vicilin, storage proteins of legume seeds , 1976 .

[4]  R. Yada,et al.  Salt-soluble seed globulins of dicotyledonous and monocotyledonous plants II. Structural characterization , 1998 .

[5]  J. Arěas,et al.  Protein-Protein Interactions in the Extrusion of Soya at Various Temperatures and Moisture Contents , 1993 .

[6]  M. Subirade,et al.  Molecular differences in the formation and structure of fine-stranded and particulate beta-lactoglobulin gels. , 2000, Biopolymers.

[7]  G. Grant,et al.  High in‐vivo (rat) digestibility of faba bean (Vicia faba), lupin (Lupinus angustifolius) and soya bean (Glycine max) soluble globulins , 1994 .

[8]  K. Murayama,et al.  Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy. , 2004, Biochemistry.

[9]  M. Lawrence,et al.  Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. , 1994, Journal of molecular biology.

[10]  K. Brew,et al.  Crystal Structures of Apo- and Holo-bovine α-Lactalbumin at 2.2-Å Resolution Reveal an Effect of Calcium on Inter-lobe Interactions* , 2000, The Journal of Biological Chemistry.

[11]  H. Mantsch,et al.  The use and misuse of FTIR spectroscopy in the determination of protein structure. , 1995, Critical reviews in biochemistry and molecular biology.

[12]  K. Das,et al.  Structural Changes of β-Lactoglobulin during Thermal Unfolding and Refolding – An FT-IR and Circular Dichroism Study , 2005, The protein journal.

[13]  B. Eggum.  Comments on Report of a joint FAO/WHO expert consultation on protein quality evaluation, Rome 1990 , 1991, Zeitschrift fur Ernahrungswissenschaft.

[14]  F. Bakker,et al.  Phylogeny, function, and evolution of the cupins, a structurally conserved, functionally diverse superfamily of proteins. , 2001, Molecular biology and evolution.

[15]  M. A. Pagani,et al.  Probing structural features of water-insoluble proteins by front-face fluorescence. , 2004, Analytical biochemistry.

[16]  D. Naumann.  FT-INFRARED AND FT-RAMAN SPECTROSCOPY IN BIOMEDICAL RESEARCH , 2001 .

[17]  C. Holt,et al.  The secondary structure of milk proteins and their biological function. , 1993, Journal of dairy science.

[18]  J. Gueguen,et al.  Identification of Resistant Pea (Pisum sativum L.) Proteins in the Digestive Tract of Chickens , 1997 .

[19]  E. Carnovale,et al.  Solubility-digestibility relationship of legume proteins , 1997 .

[20]  H. Mantsch,et al.  Aggregation of chymotrypsinogen: portrait by infrared spectroscopy. , 1992, Biochimica et biophysica acta.

[21]  W. Horwitz.  Official Methods of Analysis , 1980 .

[22]  G. Grant,et al.  Heat-induced denaturation impairs digestibility of legume (Phaseolus vulgaris L and Vicia faba L) 7S and 11S globulins in the small intestine of rat , 2005 .

[23]  P. Yu.  Multicomponent Peak Modeling of Protein Secondary Structures: Comparison of Gaussian with Lorentzian Analytical Methods for Plant Feed and Seed Molecular Biology and Chemistry Research , 2005, Applied spectroscopy.

[24]  G. Grant,et al.  Perspectives into factors limiting in vivo digestion of legume proteins: antinutritional compounds or storage proteins? , 2000, Journal of agricultural and food chemistry.

[25]  C. Ma,et al.  Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry. , 2005, Journal of agricultural and food chemistry.

[26]  W. Kabsch,et al.  Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.

[27]  Darren R. Flower,et al.  Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalin , 1997 .

[28]  J. Bandekar,et al.  Amide modes and protein conformation. , 1992, Biochimica et biophysica acta.

[29]  A. McPherson,et al.  The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 A resolution. , 2000, Acta crystallographica. Section D, Biological crystallography.

[30]  S. Utsumi.  Plant food protein engineering. , 1992, Advances in food and nutrition research.

[31]  J. Kinsella,et al.  Structural and conformational basis of the resistance of .beta.-lactoglobulin to peptic and chymotryptic digestion , 1988 .

[32]  G. Meng,et al.  Fourier-transform infrared spectroscopic study of globulin from Phaseolus angularis (red bean). , 2001, International journal of biological macromolecules.

[33]  P. Rougé,et al.  Molecular modelling of the major peanut allergen Ara h 1 and other homotrimeric allergens of the cupin superfamily: a structural basis for their IgE-binding cross-reactivity. , 2005, Biochimie.