NDLI: Enhanced stability of heterologous proteins by supramolecular self-assembly

Content Provider	Springer Nature Link
Author	Park, Jin Seung Ahn, Ji Young Lee, Sung Hyun Lee, Hyewon Han, Kyung Yeon Seo, Hyuk Seong Ahn, Keum Young Min, Bon Hong Sim, Sang Jun Choi, Insung S. Kim, Yang Hoon Lee, Jeewon
Copyright Year	2007
Abstract	Recently, we reported on the dual function of human ferritin heavy chain (hFTN-H) used for the fusion expression and solubility enhancement of various heterologous proteins: (1) high-affinity interaction with HSP70 chaperone DnaK and (2) formation of self-assembled supramolecules with limited and constant sizes. Especially the latter, the self-assembly function of hFTN-H is highly useful in avoiding the undesirable formation of insoluble macroaggregates of heterologous proteins in bacterial cytoplasm. In this study, using enhanced green fluorescent protein (eGFP) and several deletion mutants of Mycoplasma arginine deiminase (ADI132–410) as reporter proteins, we confirmed through TEM image analysis that the recombinant fusion proteins (hFTN-H::eGFP and hFTN-H::ADI132–410) formed intracellular spherical particles with nanoscale diameter (≈10 nm), i.e., noncovalently cross-linked supramolecules. Surprisingly, the supramolecular eGFP and ADI showed much enhanced stability in bioactivity. That is, the activity level was much more stably maintained for the prolonged period of time even at high temperature, at high concentration of Gdn–HCl, and in wide range of pH. The stability enhancement by supramolecular self-assembly may make it possible to utilize the protein supramolecules as novel means for drug delivery, enzymatic material conversion (biotransformation), protein chip/sensor, etc. where the maintenance of protein/enzyme stability is strictly required.
Starting Page	347
Ending Page	355
Page Count	9
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	75
Issue Number	2
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2007-02-14
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Human ferritin heavy chain Self-assembly Supramolecules Enhanced stability Microbial Genetics and Genomics Microbiology Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

BIOTECHNOLOGICALLY RELEVANT ENZYMES AND PROTEINS Enhanced stability of heterologous proteins by supramolecular self-assembly

Enhanced productivity of protease-sensitive heterologous proteins by disruption of multiple protease genes in the fission yeast Schizosaccharomyces pombe

Engineering the heterologous expression of lanthipeptides in Escherichia coli by multigene assembly

Further enhanced production of heterologous proteins by double-gene disruption (ΔAosedD ΔAovps10) in a hyper-producing mutant of Aspergillus oryzae

RETRACTED ARTICLE: Strategies for efficient production of heterologous proteins in Escherichia coli

Retraction Note: Strategies for efficient production of heterologous proteins in Escherichia coli

Enhanced thermal stability and specific activity of Pseudomonas aeruginosa lipoxygenase by fusing with self-assembling amphipathic peptides

Efficient heterologous expression and secretion in Aspergillus oryzae of a llama variable heavy-chain antibody fragment VHH against EGFR

Enhanced heterologous protein productivity by genome reduction in Lactococcus lactis NZ9000

Enhanced stability of heterologous proteins by supramolecular self-assembly

Similar Documents

BIOTECHNOLOGICALLY RELEVANT ENZYMES AND PROTEINS Enhanced stability of heterologous proteins by supramolecular self-assembly

Enhanced productivity of protease-sensitive heterologous proteins by disruption of multiple protease genes in the fission yeast Schizosaccharomyces pombe

Engineering the heterologous expression of lanthipeptides in Escherichia coli by multigene assembly

Further enhanced production of heterologous proteins by double-gene disruption (ΔAosedD ΔAovps10) in a hyper-producing mutant of Aspergillus oryzae

RETRACTED ARTICLE: Strategies for efficient production of heterologous proteins in Escherichia coli

Retraction Note: Strategies for efficient production of heterologous proteins in Escherichia coli

Enhanced thermal stability and specific activity of Pseudomonas aeruginosa lipoxygenase by fusing with self-assembling amphipathic peptides

Efficient heterologous expression and secretion in Aspergillus oryzae of a llama variable heavy-chain antibody fragment VHH against EGFR

Enhanced heterologous protein productivity by genome reduction in Lactococcus lactis NZ9000

Enhanced stability of heterologous proteins by supramolecular self-assembly