A primary approach for separation and characterization of α-amylase from white pitaya (Hylocereus undatus) peels by polymer/salt two phase system

α-Amylase was isolated from white pitaya peel with two phase system in aqueous media and then characterized. The effects of polyethylene glycol (PEG), PEG concentration, molecular weight, sodium citrate, and sodium chloride (NaCl) on yield and purification factor were studied. The highest purificat...

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Main Authors: Shad, Zahra, Meor Hussin, Anis Shobirin, Akbari-adergani, Behrouz
Format: Article
Published: Faculty of Biotechnology and Food Sciences 2022
Online Access:http://psasir.upm.edu.my/id/eprint/100335/
https://office2.jmbfs.org/index.php/JMBFS/article/view/3467
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spelling my.upm.eprints.1003352024-01-29T04:39:20Z http://psasir.upm.edu.my/id/eprint/100335/ A primary approach for separation and characterization of α-amylase from white pitaya (Hylocereus undatus) peels by polymer/salt two phase system Shad, Zahra Meor Hussin, Anis Shobirin Akbari-adergani, Behrouz α-Amylase was isolated from white pitaya peel with two phase system in aqueous media and then characterized. The effects of polyethylene glycol (PEG), PEG concentration, molecular weight, sodium citrate, and sodium chloride (NaCl) on yield and purification factor were studied. The highest purification factor (4.5) and yield (83%) were obtained in system PEG 6000 (14% w/w)-sodium citrate (18% w/w) with 6% (w/w) NaCl. The purified α-amylase molecular weight exhibited a band above 40 KDa by SDS-PAGE. α-Amylase showed optimum activity at pH of 6.0 and temperature of 55 °C. The activity of this enzyme was stable in the pH scope of 6-8 and temperature scope of 10-55 °C. Various metal ions were evaluated for amylase activation/inhibition effect. Na+ and Ca2+ were exhibited to have appropriate activating effect, where as Mn2+, Zn2+, Fe3+, Ni+, Ba+ and Cu2+ had inhibition effect. In addition, this enzyme showed remarkable stability in the existence of TritonX-100, SDS, sodium perborate, Tween 20 and Tween-80. In conclusion, this enzyme has high stability and activity at suitable temperature and pH, and in the existence of different surfactants and metal ions. This approach has a potential in progress of various industrial applications by introducing a method for applying new, low-cost, and biocompatible amylases source. Faculty of Biotechnology and Food Sciences 2022-02-01 Article PeerReviewed Shad, Zahra and Meor Hussin, Anis Shobirin and Akbari-adergani, Behrouz (2022) A primary approach for separation and characterization of α-amylase from white pitaya (Hylocereus undatus) peels by polymer/salt two phase system. Journal of microbiology, biotechnology and food sciences, 11 (4). pp. 1-6. ISSN 1338-5178 https://office2.jmbfs.org/index.php/JMBFS/article/view/3467 10.55251/jmbfs.3467
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
description α-Amylase was isolated from white pitaya peel with two phase system in aqueous media and then characterized. The effects of polyethylene glycol (PEG), PEG concentration, molecular weight, sodium citrate, and sodium chloride (NaCl) on yield and purification factor were studied. The highest purification factor (4.5) and yield (83%) were obtained in system PEG 6000 (14% w/w)-sodium citrate (18% w/w) with 6% (w/w) NaCl. The purified α-amylase molecular weight exhibited a band above 40 KDa by SDS-PAGE. α-Amylase showed optimum activity at pH of 6.0 and temperature of 55 °C. The activity of this enzyme was stable in the pH scope of 6-8 and temperature scope of 10-55 °C. Various metal ions were evaluated for amylase activation/inhibition effect. Na+ and Ca2+ were exhibited to have appropriate activating effect, where as Mn2+, Zn2+, Fe3+, Ni+, Ba+ and Cu2+ had inhibition effect. In addition, this enzyme showed remarkable stability in the existence of TritonX-100, SDS, sodium perborate, Tween 20 and Tween-80. In conclusion, this enzyme has high stability and activity at suitable temperature and pH, and in the existence of different surfactants and metal ions. This approach has a potential in progress of various industrial applications by introducing a method for applying new, low-cost, and biocompatible amylases source.
format Article
author Shad, Zahra
Meor Hussin, Anis Shobirin
Akbari-adergani, Behrouz
spellingShingle Shad, Zahra
Meor Hussin, Anis Shobirin
Akbari-adergani, Behrouz
A primary approach for separation and characterization of α-amylase from white pitaya (Hylocereus undatus) peels by polymer/salt two phase system
author_facet Shad, Zahra
Meor Hussin, Anis Shobirin
Akbari-adergani, Behrouz
author_sort Shad, Zahra
title A primary approach for separation and characterization of α-amylase from white pitaya (Hylocereus undatus) peels by polymer/salt two phase system
title_short A primary approach for separation and characterization of α-amylase from white pitaya (Hylocereus undatus) peels by polymer/salt two phase system
title_full A primary approach for separation and characterization of α-amylase from white pitaya (Hylocereus undatus) peels by polymer/salt two phase system
title_fullStr A primary approach for separation and characterization of α-amylase from white pitaya (Hylocereus undatus) peels by polymer/salt two phase system
title_full_unstemmed A primary approach for separation and characterization of α-amylase from white pitaya (Hylocereus undatus) peels by polymer/salt two phase system
title_sort primary approach for separation and characterization of î±-amylase from white pitaya (hylocereus undatus) peels by polymer/salt two phase system
publisher Faculty of Biotechnology and Food Sciences
publishDate 2022
url http://psasir.upm.edu.my/id/eprint/100335/
https://office2.jmbfs.org/index.php/JMBFS/article/view/3467
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