Next Article in Journal
The CLC-2 Chloride Channel Modulates ECM Synthesis, Differentiation, and Migration of Human Conjunctival Fibroblasts via the PI3K/Akt Signaling Pathway
Next Article in Special Issue
Flavonoids as Cytokine Modulators: A Possible Therapy for Inflammation-Related Diseases
Previous Article in Journal
Reconstruction and Application of Protein–Protein Interaction Network
Previous Article in Special Issue
Nutraceutical Properties of Olive Oil Polyphenols. An Itinerary from Cultured Cells through Animal Models to Humans
Article Menu
Issue 6 (June) cover image

Export Article

Open AccessArticle

High-Level Expression of Recombinant Bovine Lactoferrin in Pichia pastoris with Antimicrobial Activity

Laboratorio de Biotecnología 1, Facultad de Ciencias Químicas, Universidad Autónoma de Chihuahua, Circuito 1, Nuevo Campus Universitario, Chihuahua CP 31125, Mexico
Laboratorio de Biotecnología, Campus de Ciencias Agropecuarias, Universidad Autónoma de Nuevo León, Francisco Villa S/N Col. Ex hacienda El Canadá, General Escobedo, Nuevo León 66054, Mexico
Author to whom correspondence should be addressed.
Academic Editors: Ana Maria Gómez Caravaca and Antonio Segura-Carretero
Int. J. Mol. Sci. 2016, 17(6), 902;
Received: 29 April 2016 / Revised: 1 June 2016 / Accepted: 1 June 2016 / Published: 9 June 2016
(This article belongs to the Special Issue Advances in Molecular Research of Functional and Nutraceutical Food)
PDF [1610 KB, uploaded 9 June 2016]


In this study, bovine lactoferrin (bLf), an iron-binding glycoprotein considered an important nutraceutical protein because of its several properties, was expressed in Pichia pastoris KM71-H under AOX1 promoter control, using pJ902 as the recombinant plasmid. Dot blotting analysis revealed the expression of recombinant bovine lactoferrin (rbLf) in Pichia pastoris. After Bach fermentation and purification by molecular exclusion, we obtained an expression yield of 3.5 g/L of rbLf. rbLf and predominantly pepsin-digested rbLf (rbLfcin) demonstrated antibacterial activity against Escherichia coli (E. coli) BL21DE3, Staphylococcus aureus (S. aureus) FRI137, and, in a smaller percentage, Pseudomonas aeruginosa (Ps. Aeruginosa) ATCC 27833. The successful expression and characterization of functional rbLf expressed in Pichia pastoris opens a prospect for the development of natural antimicrobial agents produced recombinantly. View Full-Text
Keywords: recombinant bovine lactoferrin; lactoferricin; antibacterial activity; Pichia pastoris recombinant bovine lactoferrin; lactoferricin; antibacterial activity; Pichia pastoris

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Iglesias-Figueroa, B.; Valdiviezo-Godina, N.; Siqueiros-Cendón, T.; Sinagawa-García, S.; Arévalo-Gallegos, S.; Rascón-Cruz, Q. High-Level Expression of Recombinant Bovine Lactoferrin in Pichia pastoris with Antimicrobial Activity. Int. J. Mol. Sci. 2016, 17, 902.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top