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Evaluation of Extraction Methods for Trypsin Enzymes From Corn Using a Colourimetric Protein Assay - Literature review Example

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The paper "Evaluation of Extraction Methods for Trypsin Enzymes From Corn Using a Colourimetric Protein Assay" is an outstanding example of a biology literature review. This chapter entails the review of the methods of trypsin enzyme extraction from corn. It incorporates the analysis of the processes right from the growing, harvesting, preparation, extraction and purification…
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The paper "Evaluation of Extraction Methods for Trypsin Enzymes From Corn Using a Colourimetric Protein Assay" is an outstanding example of a biology literature review. This chapter entails the review of the methods of trypsin enzyme extraction from corn. It incorporates the analysis of the processes right from the growing, harvesting, preparation, extraction and purification. Among the processes and methods that will be discussed are extraction methods; Solid Phase Extraction (SPE), purification methods; affinity chromatography, ion-exchange chromatography, methods of analysis; Colourimetric Protein Assay Bicinchoninic Acid (BCA) and Sulfate polyacrylamide gel electrophoresis (SDS PAGE).

2.1 Trypsin Enzymes

According to Underkofler et al (1957), enzymes are biocatalysts that are produced by different living cells so as to facilitate specific biochemical reactions that form part of cells’ metabolic processes. Enzymes are specific in action on various substrates and as such a number of various enzymes are needed to bring about the sequence of various metabolic reactions that are carried out by living cells. Enzymes are proteins in nature and may or may not contain a prosthetic group. Trypsin is produced by animals, plants and bacteria. In humans, it is produced in its inactive form trypsinogen. Trypsin follows under the category of proteases. It has been noted that proteolytic enzymes are a mixture of exopeptidases and endopeptidases (proteinases). Endopeptidases breakdown proteins into proteoses, peptones and polypeptides while exopeptidases breakdown proteoses, polypeptides and peptones into amino acids.

Trypsin has found use in the pharmaceutical industry, as a digestive aid, commercial protein processing, detergent additives, leather processing, eye care products, commercial cell culture, as wound debridement, inflammation, injection of bruises and the clinical industry (Woodward). Its various uses have led to the need for its commercial production and as such the use of transgene proteins for instance corn.

Protease Inhibitors

Wati et al (2009) define protease inhibitors as minute protein molecules that have the capability to stop the action of various proteolytic enzymes. They are obtained from most organisms especially in plants where they are majorly found.

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