TY - JOUR
T1 - Characterization of Structural Changes of Casein Micelles at Different pH Using Microscopy and Spectroscopy Techniques
AU - Rojas-Candelas, Liliana Edith
AU - Chanona-Pérez, José Jorge
AU - Méndez, Juan Vicente Méndez
AU - Morales-Hernández, José Antonio
AU - Benavides, Héctor Alfredo Calderón
N1 - Publisher Copyright:
Copyright © The Author(s), 2022. Published by Cambridge University Press on behalf of the Microscopy Society of America.
PY - 2022/4/28
Y1 - 2022/4/28
N2 - 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.
AB - 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.
KW - Raman spectroscopy
KW - atomic force microscopy
KW - casein micelle structure
KW - cryo-transmission electron microscopy
KW - multivariate analysis
UR - http://www.scopus.com/inward/record.url?scp=85124962427&partnerID=8YFLogxK
U2 - 10.1017/S1431927622000162
DO - 10.1017/S1431927622000162
M3 - Artículo
C2 - 35156608
AN - SCOPUS:85124962427
SN - 1431-9276
VL - 28
SP - 527
EP - 536
JO - Microscopy and Microanalysis
JF - Microscopy and Microanalysis
IS - 2
ER -