Study of pH and Thermodynamic Parameters via Circular Dichroism Spectroscopy of a Recombinant Human Lactoferrin

Author:

Álvarez-Mayorga Beatriz L.1ORCID,Romero-Gómez Sergio1ORCID,Rosado Jorge L.2ORCID,Ocampo-Hernández Janet3ORCID,Gómez-Guzmán J.3ORCID,Ortiz-Frade Luis3ORCID

Affiliation:

1. Facultad de Química, Universidad Autónoma de Querétaro, Queretaro 76010, Mexico

2. Departamento de Nutrición Humana, Facultad de Ciencias Naturales, Universidad Autónoma de Querétaro, Queretaro 76230, Mexico

3. Departamento de Electroquímica, Centro de Investigación y Desarrollo Tecnológico en Electroquímica S.C. Parque Tecnológico Querétaro, Sanfandila, Queretaro 76703, Mexico

Abstract

The production of human recombinant proteins to be used for therapeutic or nutritional purposes must focus on obtaining a molecule that is as close as possible to the native human protein. This biotechnological tool has been documented in various studies published in recent decades, with lactoferrin being one of those that has generated the most interest, being a promising option for recombinant technology. However, stability studies including thermodynamic parameters have not been reported for recombinant lactoferrin (Lf). The objective of this work was to obtain the human recombinant protein using the yeast Komagataella phaffii to study structural changes modifying pH and temperature using circular dichroism spectroscopy (CD). Thermodynamic parameters such as ΔH, ΔS and Tm were calculated and compared with commercial human lactoferrin. We propose the potential use of CD and thermodynamic parameters as a criterion in the production of recombinant proteins to be used in the production of specialized recombinant proteins.

Publisher

MDPI AG

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