Intensified expression and purification of a recombinant biosurfactant protein

Dwyer, Mirjana Dimitrijev; Brech, Michael; Yu, Lei; Middelberg, Anton P. J.

doi:10.1016/j.ces.2013.10.024

Cited by 30 publications

(37 citation statements)

References 73 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Highly pure fusion protein DAMP4 var -pexiganan was obtained at high yield (around 24 mg per 800 mL cell culture with a final cultivation OD 600 ~ 2). The purification yield of DAMP4 var -pexiganan protein is increased twofold with a 72.9% of the protein recovery in this study as compared to the previous purification processes (Dwyer in Chem Eng Sci 105:12–21, 2014). The antimicrobial peptide pexiganan was released and activated from the fusion protein by a simple acid-cleavage.…”

mentioning

confidence: 62%

“…This paper presents a new downstream processing method to produce antimicrobial peptides from recombinant E. coli based on selective thermochemical lysis (Dwyer et al 2014) and precipitation (Wibowo et al 2017) methods. This method relies on the superior thermal and chemical stability of a four helix bundle protein DAMP4.…”

Section: Discussionmentioning

confidence: 99%

“…In addition to its surface activity, DAMP4 protein can be easily produced in recombinant E. coli at high-expression yield and high solubility in a simple buffer, and DAMP4′s four-helix bundle structure in bulk solution makes it stable and soluble under high temperature and high salt concentration (Dwyer et al 2014). These unique properties allow the high-yield purification of DAMP4 proteins with high purity by using precipitation-based methods (Dwyer et al 2014; Zhao et al 2015). …”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Cost-effective downstream processing of recombinantly produced pexiganan peptide and its antimicrobial activity

et al. 2018

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) have significant potential as alternatives to classical antibiotics. However, AMPs are currently prepared using processes which are often laborious, expensive and of low-yield, thus hindering their research and application. Large-scale methods for production of AMPs using a cost-effective approach is urgently required. In this study, we report a scalable, chromatography-free downstream processing method for producing an antimicrobial peptide, pexiganan, using recombinant Escherichia coli (E. coli). The four helix bundle structure of the unique carrier protein DAMP4 was used to facilitate a simple and cheap purification process based on a selective thermochemical precipitation. Highly pure fusion protein DAMP4var-pexiganan was obtained at high yield (around 24 mg per 800 mL cell culture with a final cultivation OD600 ~ 2). The purification yield of DAMP4var-pexiganan protein is increased twofold with a 72.9% of the protein recovery in this study as compared to the previous purification processes (Dwyer in Chem Eng Sci 105:12–21, 2014). The antimicrobial peptide pexiganan was released and activated from the fusion protein by a simple acid-cleavage. Isoelectric precipitation was then applied to separate the pexiganan peptide from the DAMP4var protein carrier. The final yield of pure bio-produced pexiganan was 1.6 mg from 800 mL of bacterial cell culture (final cultivation OD600 ~ 2). The minimum bactericidal concentration (MBC) test demonstrated that the bio-produced pexiganan has the same antimicrobial activity as chemically synthesized counterpart. This novel downstream process provides a new strategy for simple and probable economic production of antimicrobial peptides.Electronic supplementary materialThe online version of this article (10.1186/s13568-018-0541-3) contains supplementary material, which is available to authorized users.

show abstract

mentioning

confidence: 62%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cost-effective downstream processing of recombinantly produced pexiganan peptide and its antimicrobial activity

et al. 2018

View full text Add to dashboard Cite

show abstract

“…This SUPEL peptide is designed to form helix structure. The helix structure is designed in order that peptide has surfactant characteristic, depleted in water, and stable at high temperature and high salinity (Dwyer et al 2014).…”

Section: Discussionmentioning

confidence: 99%

“…MEOR is the technology using microbial and the metabolic way for oil recovery (Bachmann et al 2014). Oil recovery using microbial that is developed into biosurfactant has become advanced as seen from the numerous researches that studied and generated about biosurfactant (Desai and Banat 1997;Van Hamme et al 2003;Sandrea and Sandrea 2007;Maneerat 2005;Dwyer et al 2014;Pacheco et al 2010). Meanwhile, biosurfactant has also weakness, the quality is hard to be standardized.…”

mentioning

confidence: 99%

Construction and Expression of Single Recombinant Peptide Surfactant for EOR Application

Sari¹,

Usman²,

Rohmat³

et al. 2017

Microbiol Indones

View full text Add to dashboard Cite

Design of Stimuli‐Responsive Peptides and Proteins

Yang

Gerstweiler

et al. 2022

Adv Funct Materials

View full text Add to dashboard Cite

Stimuli‐responsive peptides and proteins are an exciting class of smart biomaterials for various applications and have received significant attention over the past decades. A wide variety of stimuli such as temperature, pH, ions, enzymes, magnetic field, redox, etc., are explored. This article provides a review of five intensively studied types of stimuli‐responsive peptides and proteins, their design principles and applications, including temperature‐, pH‐, light‐, metal ion‐, and enzyme‐responsive with an emphasis on the key design concepts and switch function. Moreover, typical examples of their applications are discussed to provide a better understanding of the design concept and underlying methodology. This review will facilitate and inspire future innovation toward new peptide‐ and protein‐based materials and their diverse applications.

show abstract

Intensified expression and purification of a recombinant biosurfactant protein

Cited by 30 publications

References 73 publications

Cost-effective downstream processing of recombinantly produced pexiganan peptide and its antimicrobial activity

Cost-effective downstream processing of recombinantly produced pexiganan peptide and its antimicrobial activity

Construction and Expression of Single Recombinant Peptide Surfactant for EOR Application

Design of Stimuli‐Responsive Peptides and Proteins

Contact Info

Product

Resources

About