Expression of recombinant amylase in Pichia Pastoris

Hazimah, Roslan (2017) Expression of recombinant amylase in Pichia Pastoris. [Final Year Project Report] (Unpublished)

[img] PDF (Please get the password by email to repository@unimas.my , or call ext: 082-583914/3973/3933)
Hazimah.pdf
Restricted to Registered users only

Download (13MB)

Abstract

Amylase is a hydrolytic enzyme that degrades starch. It is widely used in fermentation and food industries. Amylase can be found in many type of organism. Some organisms such as bacteria and fungi have extracellular enzymes secretion whereby it will secrete amylase from the cell. In this study, a recombinant amylase was transformed into yeast, Pichia pastoris, using the yeast vector, pPICZalpha. The aim of the study was to transform the recombinant amylase into P. pastoris using electroporation and to optimise the expression of the recombinant amylase using several inducing conditions. The optimisation of amylase activity was determined using DNS assay. Colony PCR was also used to check the integration of amylase in P. pastoris. Iodine staining was performed to observe protein expression after transformation. The production of recombinant amylase in yeast system have the potential to help in many application such as feedstock and food processing process.

Item Type: Final Year Project Report
Additional Information: Project Report (B.Sc.) -- Universiti Malaysia Sarawak, 2017
Uncontrolled Keywords: Pichia pastoris, Amylase, Recombinant, Universiti Malaysia Sarawak, UNIMAS, university, universiti, Borneo, Malaysia, Sarawak, Kuching, Samarahan, ipta, education, undergraduate, research, Universiti Malaysia Sarawak
Subjects: Q Science > Q Science (General)
Q Science > QR Microbiology
Divisions: Academic Faculties, Institutes and Centres > Faculty of Resource Science and Technology
Faculties, Institutes, Centres > Faculty of Resource Science and Technology
Depositing User: Unai
Date Deposited: 17 Jul 2020 06:50
Last Modified: 10 Oct 2023 07:02
URI: http://ir.unimas.my/id/eprint/30517

Actions (For repository members only: login required)

View Item View Item