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The high specificity of enzymes enables the analysis in complex sample matrixes without complicated sample preparation techniques.

White muscle disease, also known as nutritional myopathy or muscular dystrophy, is a degenerative disease of skeletal and cardiac muscles that affects all species, with particular emphasis on ruminants.

At NZYTech we intend to develop, manufacture and market solutions that simplify, accelerate and improve life sciences research. Thus, conscious of the pressures that befall on structural genomics and proteomics as a result of the dramatic increasing number of genome sequences available nowadays, we have recently developed a high-throughput (HTP) platform to efficiently clone and express a large amount of recombinant proteins that can be rapidly used in subsequent protocols for function and structure determination.

At NZYTech we are constantly developing innovative products and services in our main areas of expertise, aiming to achieve the highest standards for laboratory research and industrial analysis. We intend to serve diligently the scientific community and to provide satisfying solutions to customers worldwide. With this in mind we have recently developed a highthroughput (HTP) platform to efficiently generate hundred to thousands of expressing clones, thus leading to the rapid characterization and screening of recombinant proteins that can be applied in subsequent protocols from structure determination to industrial procedures. To achieve this, we have optimized, in a high-throughput away, most of the classical and standard methods used in molecular biology.

Efficacy of de novo gene synthesis largely depends on the quality of overlapping oligonucleotides used as template for PCR assembly. The error rate associated with current gene synthesis protocols limits the efficient and accurate production of synthetic genes, both in the small and large scales. Here, we analysed the ability of different endonuclease enzymes, which specifically recognize and cleave DNA mismatches resulting from incorrect impairments between DNA strands, to remove mutations accumulated in synthetic genes.

This study reveals that E. coli is a convenient heterologous host for the expression of soluble and functional venom peptides. Using the optimal construct design, a large and diverse range of animal venom peptides were produced in the µM scale. These results open up new possibilities for the high-throughput production of recombinant disulphide-rich peptides in E. coli.

Animal venoms are complex molecular cocktails containing a wide range of biologically active disul-

phide-reticulated peptides that target, with high selectivity and efficacy, a variety of membrane receptors. Disulphide- reticulated peptides have evolved to display improved specificity, low immunogenicity and to show much higher resistance to degradation than linear peptides.