Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Stabilization of luciferase from Renilla reniformis using random mutations.

Protein engineering, design & selection : PEDS - 1 Jan 2017

Shigehisa Megumi, Amaba Norie, Arai Shigeki, Higashi Chisato, Kawanabe Ryo, Matsunaga Ayano, Laksmi Fina Amreta, Tokunaga Masao, Ishibashi Matsujiro

Abstract excerpt

We expressed luciferase (RLuc) from Renilla reniformis in Escherichia coli RLuc was purified using a Ni-NTA column and subsequently characterized. It was unstable in acidic solutions and at 30°C. To increase the stability of RLuc, the Rluc gene was randomly mutated using error-prone polymerase chain reaction. E. coli harboring the mutated gene was screened by detecting luminescence on a plate containing the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Enzyme Stability
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutagenesis

Share to Mutation

Share to Protein Structure, Secondary

Share to Solubility

Share to Temperature

Source

Identifiers

PMID: 27881682
DOI: 10.1093/protein/gzw056

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Stabilization of luciferase from Renilla reniformis using random mutations.PMID 27881682Read ↗

Expression and characterization of the Renilla luciferase with the cumulative mutation.Semantic proximity Read ↗

Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the β-galactosidase from Bacillus subtilis VTCC-DVN-12-01.Semantic proximity Read ↗

Utilization of low-stability variants in protein evolutionary engineering.Semantic proximity Read ↗

Rational mutagenesis by engineering disulphide bonds improves Kluyveromyces lactis beta-galactosidase for high-temperature industrial applications.Semantic proximity Read ↗

Thermostabilization of firefly luciferase by in vivo directed evolution.Semantic proximity Read ↗

Tuning Thermostability and Catalytic Efficiency of Aflatoxin-Degrading Enzyme by Error-prone PCR.Semantic proximity Read ↗

Understanding the basis of thermostability for enzyme "Nanoluc" towards designing industry-competent engineered variants.Semantic proximity Read ↗

Decreasing translation error rate in Escherichia coli increases protein function.Semantic proximity Read ↗

Improved bioluminescence-based endotoxin measurement method using a salt-resistant luciferase mutant.Semantic proximity Read ↗

Improved thermostability of the North American firefly luciferase: saturation mutagenesis at position 354.Semantic proximity Read ↗

Tailoring the evolution of BL21(DE3) uncovers a key role for RNA stability in gene expression toxicity.Semantic proximity Read ↗

Highly active BRET-reporter based on yellow mutant of Renilla muelleri luciferase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.