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B-factor Guided Proline Substitutions in Chromobacterium violaceum Amine Transaminase – An Evaluation of the Proline Rule as a Method for Enzyme Stabilization
KTH, Skolan för kemi, bioteknologi och hälsa (CBH), Industriell bioteknologi.ORCID-id: 0000-0003-3073-5641
KTH, Skolan för kemi, bioteknologi och hälsa (CBH), Industriell bioteknologi.
KTH, Skolan för kemi, bioteknologi och hälsa (CBH), Industriell bioteknologi. (AlbaNova University Center)
2019 (engelsk)Inngår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 20, nr 10, s. 1297-1304Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Biocatalysis is attracting interest in the chemical industry as a sustainable alternative in large-scale chemical transformations. However, low operational stability of naturally evolved enzymes is a challenge and major efforts are required to engineer protein stability, usually by directed evolution. The development of methods for protein stabilization based on rational design is of great interest, as it would minimize the efforts needed to generate stable enzymes. We hereby present a rational design strategy based on proline substitutions in flexible areas of the protein identified by analyzing B-factors. Several proline substitutions in the amine transaminase from Chromobacterium violaceum were shown to have a positive impact on stability with increased half-life at 60°C by a factor of 2.7 (variant K69P/D218P/K304P/R432P) as well as increased melting temperature by 8.3°C (variant K167P). Finally, the presented method utilizing B-factor analysis in combination with the Proline rule was deemed successful at increasing the stability of this enzyme.

sted, utgiver, år, opplag, sider
Wiley-VCH Verlagsgesellschaft, 2019. Vol. 20, nr 10, s. 1297-1304
Emneord [en]
Biocatalysis, Enzymes, Enzyme Stabilization, Protein engineering, Molecular modeling
HSV kategori
Forskningsprogram
Bioteknologi
Identifikatorer
URN: urn:nbn:se:kth:diva-243023DOI: 10.1002/cbic.201800749ISI: 000471316400013PubMedID: 30637901Scopus ID: 2-s2.0-85063236398OAI: oai:DiVA.org:kth-243023DiVA, id: diva2:1285119
Forskningsfinansiär
Carl Tryggers foundation
Merknad

QC 20190225

Tilgjengelig fra: 2019-02-01 Laget: 2019-02-01 Sist oppdatert: 2020-03-09bibliografisk kontrollert

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