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dc.contributor.advisorChoudhury, Dr. Naiyyum
dc.contributor.authorAli, Syed Morsalin
dc.date.accessioned2018-02-01T06:40:05Z
dc.date.available2018-02-01T06:40:05Z
dc.date.issued2017
dc.identifier.otherID 12176013
dc.identifier.urihttp://hdl.handle.net/10361/9334
dc.descriptionThis thesis report is submitted in partial fulfillment of the requirement for the degree of M.Sc in Biotechnology, 2017.en_US
dc.descriptionCataloged from PDF version of thesis.
dc.descriptionIncludes bibliographical references (pages 49-53).
dc.description.abstractNowadays Yeast cell is a popular host for recombinant human insulin production where initially it secrets insulin precursor fusion protein with N-terminal spacer peptide and deletedthreonineB30, followed by a small C-peptide connected with its A andB chains. The insulin precursor is then purified and subsequently converted into human insulin ester via a slow transpeptidation reaction (hydrolysis and coupling) in presence of both trypsin and O-tert-Butyl-L-threonine –tert-butyl ester (O-Thr-ester). Transpeptidation reaction is very critical for recovery of insulin at the least expenses of the aforementioned chemicals. In this study a protocol has been developed where certain parameters have been changed in congruence with published data. The major focus was to use low amount of trypsin and O-Thr-ester for the transpeptidation reaction as well as changing organic solvent composition, water content, pH, time and temperature. In this study, a two-step transpeptidation reaction has been proposed instead of one-step reaction process by separating the cleavage step from the coupling step so that each reaction was performed under its optimal condition. Through this method, the total the conversion of insulin ester increased 57.44% and the reaction time was reduced 58.33% by using the same amount of trypsin and O-Thr-ester compared with the one-step method and available published data. Thus, this two-step transpeptidation strategy was simple, efficient, suitable for scale-up and cost effective and could be used for the pharmaceutical production of human insulin.en_US
dc.description.statementofresponsibilitySyed Morsalin Ali
dc.language.isoenen_US
dc.publisherBRAC Universityen_US
dc.rightsBRAC University thesis reports are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission.
dc.subjectInsulinen_US
dc.subjectDownstream processingen_US
dc.subjectGDMen_US
dc.subjectAdenosine triphosphateen_US
dc.subjectDiabetes mellitusen_US
dc.titleOptimization of transpeptidation reaction of the insulin precursor for efficient yield recovery during downstream processingen_US
dc.typeThesisen_US
dc.contributor.departmentDepartment of Mathematics and Natural Sciences, BRAC University
dc.contributor.department
dc.description.degreeM. Biotechnology


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