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Structural modifications of Amaranth proteins during germination.

Paula Aphalo¹, E Nora Martínez, M Cristina Añón

¹Facultad de Ciencias Exactas, Centro de Investigación y Desarrollo en Criotecnología de Alimentos (CIDCA), Universidad Nacional de La Plata y Consejo Nacional de Investigaciones Científicas y Técnicas, 1900 La Plata, Argentina.

The Protein Journal

|February 27, 2009

Summary

Amaranth storage proteins like albumins and globulins are hydrolyzed after germination. Protein mobilization order depends on aggregation and surface polypeptide susceptibility.

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Area of Science:

Plant biochemistry
Seed physiology
Protein hydrolysis

Background:

Amaranth seed storage proteins are crucial for germination and early seedling development.
Understanding the hydrolysis sequence of these proteins is key to optimizing their utilization.
Previous studies have focused on protein identification but less on their mobilization dynamics.

Purpose of the Study:

To elucidate the sequential hydrolysis of amaranth storage proteins post-germination.
To correlate protein structure, aggregation state, and polypeptide accessibility with hydrolysis patterns.
To investigate the differential mobilization of globulin fractions (7S globulin, 11S-globulin, globulin-p).

Main Methods:

Analysis of protein hydrolysis patterns during amaranth germination.
Characterization of amaranth globulin fractions (7S, 11S, globulin-p).
Assessment of polypeptide cleavage and conformational changes in storage proteins.

Main Results:

Amaranth storage proteins, including albumins and globulins, undergo hydrolysis immediately after germination.
Globulins are mobilized before glutelins, with 7S globulin and specific 11S-globulin/globulin-p polypeptides being hydrolyzed first.
Despite polypeptide cleavage, globulin molecules showed minimal size changes, though globulin-p exhibited greater conformational alterations than 11S-globulin.

Conclusions:

The order of storage protein mobilization in amaranth is determined by protein aggregation and the surface exposure of hydrolyzable polypeptides.
Globulin-p's higher susceptibility to structural changes is linked to its propolypeptide content and susceptibility to enzymatic hydrolysis.
These findings provide insights into the biochemical regulation of seed protein mobilization and its structural basis.