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Expanded popcorn grain is widely consumed as a healthy snack all around the world; however, the study of the behavior of its components by processes such as nixtamalization is scarce. Therefore, the aim of this work was to characterize the nanomechanical, structural, and antioxidant properties of nixtamalized popcorn grain pericarp. FT-IR results showed that the secondary structure of proteins of the nixtamalized pericarp was α-helix with 42.10%, the turn was 21.5% and 36.33% β-sheet, and proteins of the pericarp did not present the random coil structure. Pericarp showed antioxidant activity, as their values were 550.1 ± 2.9 and 44.2 ± 1.6 (TE)/mL for ABTS and DPPH, respectively; total phenols content was 0.21 ± 0.008 (TE)/mL; reducing power values were around 29 to 31%; hydroxyl radical scavenging ranged from 36 to 55% and iron chelation around 115 to 140% compared to the standard acids. Thickness values of the nixtamalized pericarp by SEM image analysis were 0.15 ± 0.1 mm near the pedicel inferior tip, 0.07 ± 0.01 mm at middle, and 0.03 ± 0.02 mm at upper of the grain. Young’s modulus value was 261.72 ± 23.58 MPa with a Gaussian function fitting at the distribution of all values. This research provides novel and valuable information for understanding the nanomechanical and protein arrangement, as well as and the antioxidant activity of nixtamalized popcorn grain pericarp in order to promote other processes and uses for this kind of pericarp maize.

This study aimed to evaluate the influence of pH changes on morphometric parameters of casein micelles and a general overview of their conformational structure through microscopy techniques, Raman spectroscopy and multivariate analysis. It was found that casein micelles morphology and protein secondary structure depend strongly upon pH. The changes of arithmetic average roughness (Ra), size, and shape of casein micelles at different pH are properly characterized by atomic force and cryo-transmission electron microscopy. Morphometric changes of casein micelles were correlated correctly with folding and unfolding of casein molecules as evaluated by Raman spectroscopy when the pH was varied. The novelty of this contribution consists in demonstrating that there is a close structure-functionality relationship between the morphometric parameters of proteins and their secondary structure. Knowledge about casein micelles can help improve their use of its diverse applications.

Fluorescence techniques have been widely used by scientists to reveal valuable information from biological samples, but in food science, small progress is known due to the complexity of the samples. In this study, two different biological samples, garlic skin (GS) and agave fibers (AF), were used to evaluate the techniques of confocal laser scanning microscopy (CLSM) and total internal reflection fluorescence (TIRF) microscopy, to obtain valuable information on the fiber size of the samples. A compositional characterization with calcofluor white in CLSM was achieved, but a superficial characterization of the samples with TIRF was made, evidencing fiber sizes of 398.67 ± 48.47 nm and 677.38 ± 76.88 nm for GS and AF, respectively. This work reveals that only an untreated sample can be used with the two techniques in the same microscope. In addition, it is possible to characterize the sample only using a spatial field of research and which valuable information about the structure of the material is found. This work provides the opportunity to use advanced fluorescence techniques for elucidation of structures shortly before studied with these techniques.

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