Evidence map›Paper›PMID 26522152›Full record

ArticleProteins2016

Toward rational thermostabilization of Aspergillus oryzae cutinase: Insights into catalytic and structural stability.

Abhijit N Shirke, Danielle Basore, Glenn L Butterfoss, Richard Bonneau, Christopher Bystroff, Richard A Gross

Abstract read
In one paragraph

Article in Proteins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
6.8field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 58 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Abhijit N ShirkeDepartment of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, New York.
Danielle BasoreCenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York.
Glenn L ButterfossCenter for Genomics and Systems Biology, New York University Abu Dhabi, Abu Dhabi, UAE.
Richard BonneauCenter for Genomics and Systems Biology, New York University, New York.
Christopher BystroffCenter for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York.
Richard A GrossDepartment of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, New York.
Rensselaer Polytechnic Institute · USNew York University · US

Funding

Computational design of specific binding proteins using Leave-One-OutR01GM099827 · NIGMS · RENSSELAER POLYTECHNIC INSTITUTE · PI BONDOS, SARAH E, BYSTROFF, CHRISTOPHER · 2012 to 2021
$2.9M
NIGMS NIH HHS R01 GM09982NIGMS NIH HHS R01 GM099827
6 · The paper itself

Abstract

Cutinases are powerful hydrolases that can cleave ester bonds of polyesters such as poly(ethylene terephthalate) (PET), opening up new options for enzymatic routes for polymer recycling and surface modification reactions. Cutinase from Aspergillus oryzae (AoC) is promising owing to the presence of an extended groove near the catalytic triad which is important for the orientation of polymeric chains. However, the catalytic efficiency of AoC on rigid polymers like PET is limited by its low thermostability; as it is essential to work at or over the glass transition temperature (Tg) of PET, that is, 70 °C. Consequently, in this study we worked toward the thermostabilization of AoC. Use of Rosetta computational protein design software in conjunction with rational design led to a 6 °C improvement in the thermal unfolding temperature (Tm) and a 10-fold increase in the half-life of the enzyme activity at 60 °C. Surprisingly, thermostabilization did not improve the rate or temperature optimum of enzyme activity. Three notable findings are presented as steps toward designing more thermophilic cutinase: (a) surface salt bridge optimization produced enthalpic stabilization, (b) mutations to proline reduced the entropy loss upon folding, and (c) the lack of a correlative increase in the temperature optimum of catalytic activity with thermodynamic stability suggests that the active site is locally denatured at a temperature below the Tm of the global structure.

Indexed as

Protein EngineeringAspergillus oryzaeCarboxylic Ester HydrolasesEnzyme StabilityModels, MolecularMutationPolyethylene TerephthalatesProtein ConformationProtein DenaturationTemperatureCarboxylic Ester HydrolasescutinasePolyethylene Terephthalatesesterasegreen chemistryPETpoly(ethylene terephthalate)protein designprotein engineeringRosettathermophile

Identifiers

PMID26522152
PMCPMC4715774
OpenAlexW1957423796

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.