Taylor vortex-based protein crystal nucleation enhancement and growth evaluation in batchwise and slug flow crystallizers

The utilisation of nucleation seeds, coupling nucleation and growth during crystallization and realistic continuum are currently relatively robust, reliable and scalable methods for protein crystallization optimization. Here, we design a segmented crystallization method, in which combines the characteristics of the Taylor vortex enhanced lysozyme nucleation stage. Different crystallizer are used for the growth segment so that the nucleation segment and the growth segment are organically combined during lysozyme crystallization. During the crystal growth stage, the crystallization properties of the Couette-Taylor (CT) crystallizer, mixing Tank (MT) crystallizer and tubular crystallizer were evaluated. The experimental results emphasize the importance of shear rate, temperature, and fluid velocity in the design of segment crystallization methods to obtain products with complete crystal morphology and uniform size distribution. This strategy successfully expanded the lysozyme crystallization from the original 10 mL scale to 200 mL, realized the continuous process, and providing a promising strategy for the design and operation of continuous SFC to produce high value protein crystals in the future.(c) 2023 Institution of Chemical Engineers. Published by Elsevier Ltd. All rights reserved.

Automated summary

The utilisation of nucleation seeds, coupling nucleation and growth during crystallization and realistic continuum are currently relatively robust, reliable and scalable methods for protein crystallization optimization. Here, we design a segmented crystallization method, in which combines the characteristics of the Taylor vortex enhanced lysozyme nucleation stage. This strategy successfully expanded the lysozyme crystallization from the original 10 mL scale to 200 mL, realized the continuous process, and providing a promising strategy for the design and operation of continuous SFC to produce high value protein crystals in the future.