Xylan deterioration approach: Purification and catalytic behavior optimization of a novel β-1,4-d-xylanohydrolase from Geobacillus stearothermophilus KIBGE-IB29

Zainab Bibi; Shah Ali Ul Qader; Afsheen Aman; Haneef Ur Rehman; Muhammad Asif Nawaz; Asad Karim; Irum Us Salam; Muhammad Waqas; Aysha Kamran

doi:10.1016/j.btre.2018.e00299

Xylan deterioration approach: Purification and catalytic behavior optimization of a novel β-1,4-d-xylanohydrolase from Geobacillus stearothermophilus KIBGE-IB29

Biotechnol Rep (Amst). 2018 Dec 27:21:e00299. doi: 10.1016/j.btre.2018.e00299. eCollection 2019 Mar.

Authors

Zainab Bibi¹, Shah Ali Ul Qader², Afsheen Aman³, Haneef Ur Rehman⁴, Muhammad Asif Nawaz⁵, Asad Karim⁶, Irum Us Salam¹, Muhammad Waqas¹, Aysha Kamran^{7

8}

Affiliations

¹ Department of Biotechnology, Federal Urdu University of Arts, Science and Technology (FUUAST), Gulshan-e-Iqbal Campus, Karachi, 75300, Pakistan.
² Department of Biochemistry, University of Karachi, Karachi, 75270, Pakistan.
³ The Karachi Institute of Biotechnology and Genetic Engineering (KIBGE), University of Karachi, Karachi, 75270, Pakistan.
⁴ Department of Chemistry, University of Turbat, Kech, Balochistan, Pakistan.
⁵ Department of Biotechnology, Shaheed Benazir Bhutto University, Sheringal, Dir Upper, KPK, Pakistan.
⁶ Jamil-Ur-Rahman Center for Genome Research, Dr. Punjwani Center for Molecular Medicine and Drug Research, International Center for Chemical and Biological Science (ICCBS), University of Karachi, Karachi, 75270, Pakistan.
⁷ Georg-August University School of Science (GAUSS), Georg-August-University Goettingen, Germany.
⁸ Department of Biotechnology, University of Karachi, Karachi-75270, Pakistan.

Abstract

The β-1,4-d-xylanohydrolase is an industry valuable catalytic protein and used to synthesize xylooligosaccharides and xylose. In the current study, β-1,4-d-xylanohydrolase from Geobacillus stearothermophilus KIBGE-IB29 was partially purified up to 9.5-fold with a recovery yield of 52%. It exhibited optimal catalytic activity at pH-7.0 and 50 °C within 5 min. Almost 50% activity retained at pH-4.0 to 9.0 however, 70% activity observed within the range of 40 °C to 70 °C. The β-1,4-d-xylanohydrolase showed a significant hydrolytic pattern with 48.7 kDa molecular mass. It was found that the enzymatic activity improved up to 160% with 1.0 mM ethanol. Moreover, the activity of enzyme drastically increased up to 2.3 and 1.5 fold when incubated with Tween 80 and Triton X-100 (1.0 mM), respectively. The β-1,4-d-xylanohydrolase also retained 72% activity at -80 °C after 180 days. Such a remarkable biochemical properties of β-1,4-d-xylanohydrolase make it possible to forecast its potential use in textile and food industries.

Keywords: 3′5′ dinitrosalicylic acid (PubChem CID: 11873); Ammonium sulfate (PubChem CID: 6097028); Catalysis; Characterization; Citric acid (PubChem CID: 311); Dihydrogen potassium phosphate (PubChem CID: 516951); Dipotassium hydrogen phosphate (PubChem CID: 24450); Glycine (PubChem CID: 750); Industrial use; Purification; Sodium potassium tartrate (PubChem CID: 9357); Thermal stability; Xylan (Simson Laboratories, UK) Xylose (PubChem CID: 135191); Xylanohydrolase.