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Enhancement of Mussel Adhesive Protein Production in Escherichia coli by Co‐expression of Bacterial Hemoglobin
Author(s) -
Kim Doil,
Hwang Dong Soo,
Kang Dong Gyun,
Kim Jaoon Y. H.,
Cha Hyung Joon
Publication year - 2008
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp0703477
Subject(s) - bioreactor , escherichia coli , mussel , recombinant dna , hemoglobin , fusion protein , biology , chemistry , biochemistry , microbiology and biotechnology , gene , botany , ecology
Mussel adhesive proteins (MAPs) have been considered as potential underwater and medical bioadhesives. Previously, we reported a functional expression of recombinant MAP hybrid fp‐151, which is a fusion protein with six type 1 (fp‐1) decapeptide repeats at each type 5 (fp‐5) terminus, with practical properties in Escherichia coli . In the present work, we introduced the Vitreoscilla hemoglobin (VHb) co‐expression strategy to enhance the production levels of hybrid fp‐151 since VHb has been successfully used for efficient oxygen utilization in several expression systems, including E. coli . In both batch‐type flask and fed‐batch‐type bioreactor cultures, we found that co‐expression of VHb conferred higher cell growth and hybrid fp‐151 production. Its positive effects were significantly increased in high cell density bioreactor cultures as the microaerobic environment was more quickly and severely formed. We obtained a ∼1.9‐fold higher (∼1 g/L) production of MAP fp‐151 from VHb co‐expressing cells in fed‐batch bioreactor cultures as compared to that from VHb non‐expressing cells. Collectively and regardless of the culture type, VHb co‐expression strategy was successful in enhancing the production of recombinant mussel adhesive proteins in the E. coli expression system.