Influence of Mixing Intensity on Lysozyme Crystallization in a Meso Oscillatory Flow Reactor

• Type: Article in International Scientific Journal
• Date: 2018

Authors

Filipa Castro (Author) FEUP; António Ferreira (Author) FEUP; José A. Teixeira (Author) Other; Fernando Rocha (Author) FEUP

Journal

Title: Crystal Growth & Design

Vol. 18 No. 10

Pages: 5940-5946

ISSN: 1528-7483

Publisher: American Chemical Society

Indexing

ISI Web of Knowledge - 0 Citations

ISI Web of Science

Scopus - 9 Citations

Scientific classification

CORDIS: Technological sciences > Engineering > Chemical engineering

FOS: Engineering and technology > Chemical engineering

Associated Projects

LEPABE - Laboratório de Engenharia de Processos, Ambiente, Biotecnologia e Energia

CrystalFlow - Cristalização em contínuo de princípios ativos

LEPABE-2-ECO-INNOVATION - LEPABE-2-ECO-INNOVATION

Other information

Authenticus ID: P-00P-MGX

DOI: 10.1021/acs.cgd.8b00721

Abstract (EN): The influence of mixing intensity on protein crystallization has been investigated for the first time in a meso oscillatory flow reactor (meso-OFR). For this, lysozyme crystallization was studied in batch at different oscillation amplitudes and frequencies. Turbidity was monitored over time to measure induction time and follow the crystallization process. Results suggest that the crystallization mechanism may be characterized by the occurrence of primary heterogeneous nucleation followed by attrition-induced secondary nucleation. Results also evidence the nonmonotonic dependence of both induction time and mean crystal size on mixing intensity. Indeed, results show that the two parameters decrease with increasing mixing intensity at Re-o below 189, while for further increase of Re-o both remain almost constant. Based on the literature, we suggest that such behavior may be explained by the influence of mixing intensity on protein clusters size distribution in solution. Further, induction time and mean crystal size show a stronger dependency on the oscillation amplitude compared to the oscillation frequency, in particular at the lower amplitudes. Finally, it is shown that lysozyme keeps its activity at the end of the experiments and crystal yields are quite reasonable.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 7