Surface Display—An Alternative to Classic Enzyme Immobilization

Enzyme immobilization to solid matrices often presents a challenge due to protein conformation sensitivity, desired enzyme purity, and requirements for the particular carrier properties and immobilization technique. Surface display of enzymes at the cell walls of microorganisms presents an alternati...

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Bibliographic Details
Main Authors: Mateja Lozančić, Amir Sk. Hossain, Vladimir Mrša, Renata Teparić
Format: Article
Language:English
Published: MDPI AG 2019-08-01
Series:Catalysts
Subjects:
Online Access:https://www.mdpi.com/2073-4344/9/9/728
Description
Summary:Enzyme immobilization to solid matrices often presents a challenge due to protein conformation sensitivity, desired enzyme purity, and requirements for the particular carrier properties and immobilization technique. Surface display of enzymes at the cell walls of microorganisms presents an alternative that has been the focus of many research groups worldwide in different fields, such as biotechnology, energetics, pharmacology, medicine, and food technology. The range of systems by which a heterologous protein can be displayed at the cell surface allows the appropriate one to be found for almost every case. However, the efficiency of display systems is still quite low. The most frequently used yeast for the surface display of proteins is <i>Saccharomyces cerevisiae</i>. However, apart from its many advantages, <i>Saccharomyces cerevisiae</i> has some disadvantages, such as low robustness in industrial applications, hyperglycosylation of some heterologous proteins, and relatively low efficiency of surface display. Thus, in the recent years the display systems for alternative yeast hosts with better performances including <i>Pichia pastoris, Hansenula polymorpha, Blastobotrys adeninivorans, Yarrowia lipolytica, Kluyveromyces marxianus</i>, and others have been developed. Different strategies of surface display aimed to increase the amount of displayed protein, including new anchoring systems and new yeast hosts are reviewed in this paper.
ISSN:2073-4344