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

Impact of the tryptophan residues of Humicola lanuginosa lipase on its thermal stability.

Biochimica et biophysica acta - 11 Jun 2001

Zhu K, Jutila A, Tuominen E K, Patkar S A, Svendsen A, Kinnunen P K

Abstract excerpt

Thermal stability of wild type Humicola lanuginosa lipase (wt HLL) and its two mutants, W89L and the single Trp mutant W89m (W117F, W221H, and W260H), were compared. Differential scanning calorimetry revealed unfolding of HLL at T(d)=74.4 degrees C whereas for W89L and W89m this endotherm was decreased to 68.6 and 62 degrees C, respectively, demonstrating significant contribution of the above Trp residues to the...

Read the complete abstract on PubMed

Topics

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

Share to Calorimetry, Differential Scanning
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Hot Temperature

Share to Lipase

Share to Spectrometry, Fluorescence

Share to Thermodynamics

Share to Tryptophan

Source

Identifiers

PMID: 11410289
DOI: 10.1016/s0167-4838(01)00198-4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Impact of the tryptophan residues of Humicola lanuginosa lipase on its thermal stability.PMID 11410289Read ↗

Steady state and time resolved effects of guanidine hydrochloride on the structure of Humicola lanuginosa lipase revealed by fluorescence spectroscopy.Semantic proximity Read ↗

Manipulation of the conformation and enzymatic properties of T1 lipase by site-directed mutagenesis of the protein core.Semantic proximity Read ↗

Differential adsorption of variants of the Thermomyces lanuginosus lipase on a hydrophobic surface suggests a role for local flexibility.Semantic proximity Read ↗

Discovery of the Key Mutation Site Influencing the Thermostability of Thermomyces lanuginosus Lipase by Rosetta Design Programs.Semantic proximity Read ↗

Histidine substitution in the most flexible fragments of firefly luciferase modifies its thermal stability.Semantic proximity Read ↗

Single-Particle Tracking of Thermomyces lanuginosus Lipase Reveals How Mutations in the Lid Region Remodel Its Diffusion.Semantic proximity Read ↗

The effect of mutations in the lid region of Thermomyces lanuginosus lipase on interactions with triglyceride surfaces: A multi-scale simulation study.Semantic proximity Read ↗

Zinc in lipase L1 from Geobacillus stearothermophilus L1 and structural implications on thermal stability.Semantic proximity Read ↗

Engineering of Bacillus lipase by directed evolution for enhanced thermal stability: effect of isoleucine to threonine mutation at protein surface.Semantic proximity Read ↗

Altering the activation mechanism in Thermomyces lanuginosus lipase.Semantic proximity Read ↗

Tryptophan Fluorescence Yields and Lifetimes as a Probe of Conformational Changes in Human Glucokinase.Semantic proximity Read ↗

Mutations in the "lid" region affect chain length specificity and thermostability of a Pseudomonas fragi lipase.Semantic proximity Read ↗

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