Optimization Production of an Endo-β-1,4-Xylanase from Streptomyces thermocarboxydus Using Wheat Bran as Sole Carbon Source

Author:

Tran Thi Ngoc1ORCID,Doan Chien Thang1ORCID,Dinh Thi Kieu Loan2,Duong Thi Hai Ninh1,Phan Thi Thuc Uyen1,Le Thi Thuy Loan1,Tran Trung Dung1,Hoang Pham Hung Quang1,Nguyen Anh Dzung3ORCID,Wang San-Lang45ORCID

Affiliation:

1. Faculty of Natural Science and Technology, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam

2. Faculty of Education, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam

3. Institute of Biotechnology and Environment, Tay Nguyen University, Buon Ma Thuot 630000, Vietnam

4. Department of Chemistry, Tamkang University, New Taipei City 25137, Taiwan

5. Life Science Development Center, Tamkang University, New Taipei City 25137, Taiwan

Abstract

Xylanases, key enzymes for hydrolyzing xylan, have diverse industrial applications. The bioprocessing of agricultural byproducts to produce xylanase through fermentation approaches is gaining importance due to its significant potential to reduce enzyme production costs. In this work, the productivity of Streptomyces thermocarboxydus TKU045 xylanase was enhanced through liquid fermentation employing wheat bran as the sole carbon source. The maximum xylanase activity (25.314 ± 1.635 U/mL) was obtained using the following optima factors: 2% (w/v) wheat bran, 1.4% (w/v) KNO3, an initial pH of 9.8, an incubation temperature of 37.3 °C, and an incubation time of 2.2 days. Xylanase (Xyn_TKU045) of 43 kDa molecular weight was isolated from the culture supernatant and was biochemically characterized. Analysis through liquid chromatography with tandem mass spectrometry revealed a maximum amino acid identity of 19% with an endo-1,4-β-xylanase produced by Streptomyces lividans. Xyn_TKU045 exhibited optimal activity at pH 6, with remarkable stability within the pH range of 6.0 to 8.0. The enzyme demonstrated maximum efficiency at 60 °C and considerable stability at ≤70 °C. Mg2+, Mn2+, Ba2+, Ca2+, 2-mercaptoethanol, Tween 20, Tween 40, and Triton X-100 positively influenced Xyn_TKU045, while Zn2+, Fe2+, Fe3+, Cu2+, and sodium dodecyl sulfate exhibited adverse impact. The kinetic properties of Xyn_TKU045 were a Km of 0.628 mg/mL, a kcat of 75.075 s−1 and a kcat/Km of 119.617 mL mg−1s−1. Finally, Xyn_TKU045 could effectively catalyze birchwood xylan into xylotriose and xylobiose as the major products.

Funder

National Science and Technology Council, Taiwan

Tay Nguyen University

Publisher

MDPI AG

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