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Role of Engineered Proteins as Therapeutic Formulations
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Khushboo Gulati, Krishna Mohan Poluri
Directed evolution (DE) is a strategy to engineer proteins based on the nature’s theme of evolution. However, DE evolves proteins with desirable traits in few days or months in comparison to millions of years for them to evolve under natural selection pressures. DE aims at exploring the sequence space which has not been scrutinized by the nature. DE has emerged as a versatile tool to tailor or alter the desired properties in numerous proteins for the wide range of biological applications with desired physicochemical and pharmacokinetic properties. The DE methodologies have not only flourished in the era of protein designing but are also being employed to engineer novel pathways, viruses, operons, and even whole microbes (Cobb et al., 2012; Cobb et al., 2013a; Cobb et al., 2013b).
Bioengineering Approach on Terpenoids Production
Published in Dijendra Nath Roy, Terpenoids Against Human Diseases, 2019
Two broad approaches have proved quite effective for improving the activity of enzymes, namely, directed evolution and rational design. Directed evolution is inspired by natural evolution whereby genetic diversity is created by mutagenesis and protein variants with desired functions are identified. Rational design method requires enough prior knowledge about the enzyme in terms of structure–function relationships to predict which mutations would result in the enhancement of enzyme activity. Lately, with the advent of powerful computing tools and the increasing amount of protein structures available, both these approaches have been combined and the combination is now referred to as ‘semi-rational design’. It involves site saturation mutagenesis or random mutagenesis over a specific part of the enzyme rather than over the entire enzyme (Porter et al. 2016).
Protein Engineering and Bionanotechnology
Published in Anil Kumar Anal, Bionanotechnology, 2018
Directed evolution is one of the most powerful protein engineering methods, which is used to redesign the protein structure to modify or create new protein with desired attribute, for instance, improving the stability or activity of enzyme under extreme condition through multiple mutations. In this method, random or focused mutagenesis and selection are proven to be effective even under the condition of limited information regarding the structure and mechanism of protein (Verma et al. 2012). Conventionally, directed evolution consists of two steps: (1) the first step is to produce molecular variety by random mutagenesis and DNA recombination and (2) the second step is applying high-throughput screening to identify the proper sequences for their functionalities (Figure 4.2). There is availability of protein library with collection of information of millions of proteins. Modern approaches based on available protein structure, sequence, and function together with computational predictive algorithms are being utilized for protein engineering (Lutz 2010).
Evaluation of droplet-based microfluidic platforms as a convenient tool for lipases and esterases assays
Published in Preparative Biochemistry and Biotechnology, 2019
Pawel Jankowski, Adam Samborski, Ryszard Ostaszewski, Piotr Garstecki
Enzymes catalyze a variety of organic and biochemical reactions. Consequently, the determination of the enzyme activity is extremely important in medical diagnostics, in biotechnology, and in research. The most important property of all enzymes is their catalytic power – measured by the kinetic parameters of an enzymatic reaction. Measurement of rapid enzyme kinetics is essential to an understanding of many biological and chemical processes.[1] Special attention has been paid to hydrolytic enzymes due to their ability to accept a wide range of substrates and to their stability in aqueous environments. Interestingly, hydrolases may also be active in organic solvents. This makes hydrolases attractive both in academic research and in industrial applications. Often, the kinetic properties of hydrolases do not meet the requirements of a particular application. Directed evolution techniques are widely used for the generation of enzymes expressing desired kinetic properties in respect to particular substrates.[2] Fast and efficient test methods for the determination of hydrolase hydrolytic activity are very valuable for high-throughput screening in biotechnology.
Design of artificial cells: artificial biochemical systems, their thermodynamics and kinetics properties
Published in Egyptian Journal of Basic and Applied Sciences, 2022
Adamu Yunusa Ugya, Lin Pohan, Qifeng Wang, Kamel Meguellati
The interactions between biomolecules, metabolism from the mitochondrial factory, and the cell membrane give birth to cellular life. Cells need a set of information carriers and metabolic reactions to become functional in a changing environment. In the last century, discovery-driven biology as well as hypothesis-driven biology to design and control the new cellular functions and genetic circuits that trigger synthetic biology has been emerging domains [1]. The complex network of interactions that drives life includes key features such as docking, adaptive systems, embedding, exchange, tethering, programs, non-covalent interactions, covalent linkages, and out of equilibrium and equilibrium states, self-replicative systems, self-organized and self-assembled systems, etc. The exploration and application of these interactions have led to the emergence of synthetic biology [2]. The field of synthetic biology is mainly divided into two branches; first by synthetic protocell biology (SPB), where the synthetic units are assembled into chemical systems endued with inheritance, evolution, and reproduction (biological properties) [3]. The second branch deals with the extraction and assembly of biological units from living systems to obtain a modified version of existing biological systems. The last one deals with the generation and rewiring of genetic circuits using elementary building blocks [4]. One of the goals driven by these research branches is to obtain a programmable plug-in genetic device [5], either by directed evolution techniques [6] or by rational design [7]. Chang (1957) was the first to propose the concept of artificial cells [8]. The studies of primordial cells [9] co-translational insertion of membrane proteins into liposomes [10] and delivery of drugs [11] are a few examples of applications made by the use of artificial cells in biotechnology and industrial field.