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Heterologous, Expression, and Characterization of Thermostable Glucoamylase Derived from Aspergillus flavus NSH9 in Pichia pastoris.
Karim, Kazi Muhammad Rezaul; Husaini, Ahmad; Hossain, Md Anowar; Sing, Ngieng Ngui; Mohd Sinang, Fazia; Hussain, Mohd Hasnain Md; Roslan, Hairul Azman.
Afiliación
  • Karim KM; Department of Molecular Biology, Faculty of Resource Science and Technology, Universiti Malaysia Sarawak, 94300 Kota Samarahan, Sarawak, Malaysia; Institute of Nutrition and Food Science, University of Dhaka, Dhaka 1000, Bangladesh.
  • Husaini A; Department of Molecular Biology, Faculty of Resource Science and Technology, Universiti Malaysia Sarawak, 94300 Kota Samarahan, Sarawak, Malaysia.
  • Hossain MA; Department of Biochemistry and Molecular Biology, University of Rajshahi, Rajshahi 6205, Bangladesh.
  • Sing NN; Department of Molecular Biology, Faculty of Resource Science and Technology, Universiti Malaysia Sarawak, 94300 Kota Samarahan, Sarawak, Malaysia.
  • Mohd Sinang F; Department of Molecular Biology, Faculty of Resource Science and Technology, Universiti Malaysia Sarawak, 94300 Kota Samarahan, Sarawak, Malaysia.
  • Hussain MH; Department of Molecular Biology, Faculty of Resource Science and Technology, Universiti Malaysia Sarawak, 94300 Kota Samarahan, Sarawak, Malaysia.
  • Roslan HA; Department of Molecular Biology, Faculty of Resource Science and Technology, Universiti Malaysia Sarawak, 94300 Kota Samarahan, Sarawak, Malaysia.
Biomed Res Int ; 2016: 5962028, 2016.
Article en En | MEDLINE | ID: mdl-27504454
A novel thermostable glucoamylase cDNA without starch binding domain (SBD) of Aspergillus flavus NSH9 was successfully identified, isolated, and overexpressed in Pichia pastoris GS115. The complete open reading frame of glucoamylase from Aspergillus flavus NSH9 was identified by employing PCR that encodes 493 amino acids lacking in the SBD. The first 17 amino acids were presumed to be a signal peptide. The cDNA was cloned into Pichia pastoris and the highest expression of recombinant glucoamylase (rGA) was observed after 8 days of incubation period with 1% methanol. The molecular weight of the purified rGA was about 78 kDa and exhibited optimum catalytic activity at pH 5.0 and temperature of 70°C. The enzyme was stable at higher temperature with 50% of residual activity observed after 20 min at 90°C and 100°C. Low concentration of metal (Mg(++), Fe(++), Zn(++), Cu(++), and Pb(++)) had positive effect on rGA activity. This rGA has the potential for use and application in the saccharification steps, due to its thermostability, in the starch processing industries.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Pichia / Aspergillus flavus / Ingeniería de Proteínas / Glucano 1,4-alfa-Glucosidasa Idioma: En Revista: Biomed Res Int Año: 2016 Tipo del documento: Article País de afiliación: Bangladesh Pais de publicación: Estados Unidos
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Pichia / Aspergillus flavus / Ingeniería de Proteínas / Glucano 1,4-alfa-Glucosidasa Idioma: En Revista: Biomed Res Int Año: 2016 Tipo del documento: Article País de afiliación: Bangladesh Pais de publicación: Estados Unidos