Mechanical Characterization of Protein Crystals

Article

Tait, Stephan, White, Edward T. and Litster, James D.. 2008. "Mechanical Characterization of Protein Crystals." Particle and Particle Systems Characterization. 25 (3), pp. 266-276. https://doi.org/10.1002/ppsc.200701112
Article Title

Mechanical Characterization of Protein Crystals

ERA Journal ID3913
Article CategoryArticle
AuthorsTait, Stephan (Author), White, Edward T. (Author) and Litster, James D. (Author)
Journal TitleParticle and Particle Systems Characterization
Journal Citation25 (3), pp. 266-276
Number of Pages11
Year2008
Place of PublicationGermany
ISSN0934-0866
1521-4117
Digital Object Identifier (DOI)https://doi.org/10.1002/ppsc.200701112
Web Address (URL)https://onlinelibrary.wiley.com/doi/10.1002/ppsc.200701112
Abstract

The mechanical properties (critical stress intensity factor, hardness and Young's modulus) of 4 crystalline materials (two proteins, lysozyme and glucose isomerase and two non-proteins, glutamic acid and potassium sulphate) were measured with an indentation technique. It was found that the mechanical properties of lysozyme crystals depend on their state – dried, partly dried and moisture saturated – and their surroundings. The hardness, Young's modulus and the critical stress intensity factor of lysozyme crystals were observed to be much lower than those for the tested non-proteins, leading to the conclusion that crystalline lysozyme is comparatively more fragile and softer. In combination the mechanical properties of lysozyme and the non-proteins indicated that these materials were fairly brittle. Mechanical properties for crystals of the other protein, glucose isomerase, could not be quantified by indentation. However, qualitatively crystalline glucose isomerase was found to be more ductile and less fragile than crystalline lysozyme. The experimental findings were interpreted in terms of relative susceptibility to attrition and secondary nucleation in stirred industrial crystallizers.

KeywordsFracture toughness; Hardness; Indentation; Protein crystallization; Secondary nucleation
ANZSRC Field of Research 2020400406. Powder and particle technology
Byline AffiliationsUniversity of Queensland
Institution of OriginUniversity of Southern Queensland
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