Microbiology Indonesia
Vol. 10 No. 1 (2016): March 2016

Heterologous Expression of α-Amylase from Saccharomycopsis fibuligera R64 and its Tyr401Trp Mutant in Pichia pastoris

RIEZKI AMALIA (Unknown)
WANGSA TIRTA ISMAYA (Dexa Laboratories of Molecular Sciences)
FERNITA PUSPASARI (Unknown)
KHOMAINI HASAN (Unknown)
TOTO SUBROTO (Unknown)
DESSY NATALIA (Unknown)
SOETIJOSO SOEMITRO (Unknown)

Article Info

Publish Date
18 Jul 2016

Abstract

α-Amylase from Saccharomycopsis fibuligera R64 is a non-adsorbing raw-starch degrading enzyme, a unique characteristic. This character is difficult to explain in the absence of its three-dimensional structure. Here we discuss the expression of a-amylase from Saccharomycopsis fibuligera in Pichia pastoris and the effect of site directed mutagenesis on its activity. A model based on the structure of its homologs suggested mutation of codon of Tyr401 into that of a Trp residue. An activity study using whole cells P. pastoris showed similar substrate degradation rates by cells carrying either the native or mutant amylase encoding gene. However, the purified enzyme of the mutant strain showed faster starch hydrolysis.

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Journal Info
Microbiology Indonesia
Website

Abbrev

mionline

Publisher

Perhimpunan Mikrobiologi Indonesia

Subject

Biochemistry, Genetics & Molecular Biology Immunology & microbiology Medicine & Pharmacology

Description

Microbiology Indonesia provides a unique venue for publishing original researches in microbiology (espesially from Indonesian reseachers), and ensures that authors could reach the widest possible audience. Microbiology Indonesia publishes a wide range of research disciplines on bacteria, archaea, ...