TY - JOUR
T1 - Characterization of protease activities in a crude extract of germinated cacao
AU - Sánchez-Mundo, M. L.
AU - Bautista-Muñoz, C.
AU - Jaramillo-Flores, M. E.
N1 - Publisher Copyright:
© 2015 The Author(s). Published by Taylor & Francis.
PY - 2015/10/2
Y1 - 2015/10/2
N2 - Dynamic light scattering (DLS) was applied to the analysis of the hydrodynamic diameter distribution of proteins in extract of germinated cacao. The interactions among divalent cations and their relation with the activity of Xaa-prolyl dipeptidyl aminopeptidase 2 (Xaa-Pro-DAP2) enzyme were evaluated. The peptidases were isolated by 80% saturation of ammonium sulfate from acetone extract of germinated cacao seeds. The results showed a higher activity of Xaa-Pro-DAP2, besides aminopeptidase (APE) and carboxypeptidase (CP) enzymes. Using DLS analysis the size distribution was found to be multi-modal; however with Cu2+ and Cd2+ at 1 mM, the size distribution was found to be monomodal with a hydrodynamic diameter of 158.5 and 119 nm, respectively. The distribution remained constant from 60 to 80°C, suggesting that thermal stability is related to increase in Xaa-Pro-DAP2 activity an lower protein aggregation. APE activity was slightly activated by Co2+ at 1 mM, whereas no significant effect was observed on CP activity.
AB - Dynamic light scattering (DLS) was applied to the analysis of the hydrodynamic diameter distribution of proteins in extract of germinated cacao. The interactions among divalent cations and their relation with the activity of Xaa-prolyl dipeptidyl aminopeptidase 2 (Xaa-Pro-DAP2) enzyme were evaluated. The peptidases were isolated by 80% saturation of ammonium sulfate from acetone extract of germinated cacao seeds. The results showed a higher activity of Xaa-Pro-DAP2, besides aminopeptidase (APE) and carboxypeptidase (CP) enzymes. Using DLS analysis the size distribution was found to be multi-modal; however with Cu2+ and Cd2+ at 1 mM, the size distribution was found to be monomodal with a hydrodynamic diameter of 158.5 and 119 nm, respectively. The distribution remained constant from 60 to 80°C, suggesting that thermal stability is related to increase in Xaa-Pro-DAP2 activity an lower protein aggregation. APE activity was slightly activated by Co2+ at 1 mM, whereas no significant effect was observed on CP activity.
KW - cacao
KW - crude extract
KW - dynamic light scattering
KW - proteases
UR - http://www.scopus.com/inward/record.url?scp=84941259919&partnerID=8YFLogxK
U2 - 10.1080/19476337.2015.1023359
DO - 10.1080/19476337.2015.1023359
M3 - Artículo
SN - 1947-6337
VL - 13
SP - 578
EP - 587
JO - CYTA - Journal of Food
JF - CYTA - Journal of Food
IS - 4
ER -