Xylanase Production by Aspergillus niger Using Agro-Industrial Residues and Tween Surfactants: A Non-Parametric Analysis
DOI:
https://doi.org/10.33795/jtkl.v10i1.8854Keywords:
Aspergillus niger, Kruskal-Wallis, palm kernel cake, sugarcane bagasse, surfactant, xylanaseAbstract
Xylanase plays a key role in hydrolyzing xylan, yet large-scale enzyme production remains limited by the high cost of purified xylan substrates. Although lignocellulosic agricultural residues offer a promising low-cost alternative, their effectiveness as substrates for Aspergillus niger and the influence of process additives on enzyme performance are not fully understood. This study addresses this gap by evaluating sugarcane bagasse and palm kernel cake as economical substrates and examining how substrate type, substrate concentration, and surfactant selection affect xylanase specific activity. Fermentation experiments were conducted using substrate concentrations of 1.5–3.0% (w/v) supplemented with Tween 20, Tween 60, or Tween 80, followed by statistical analysis using the Kruskal–Wallis test and Bonferroni-corrected Mann–Whitney U tests. Substrate concentration (p = 0.016) and surfactant type (p < 0.001) significantly influenced specific activity, whereas substrate type did not (p = 0.224). The highest activity (4.380 ± 0.052 IU/mg; median = 1.9113) was achieved using 3.0% palm kernel cake with Tween 20. These findings demonstrate that optimizing substrate load and surfactant choice is crucial for enhancing xylanase production from low-cost agro-industrial residues, providing practical insights for cost-efficient enzyme bioprocess development.
References
N. Bhardwaj, B. Kumar, P. Verma, A detailed overview of xylanases: an emerging biomolecule for current and future prospective, Bioresour. Bioprocess. 6 (2019) 40.
S.B. Ajeje, Y. Hu, G. Song, S.B. Peter, R.G. Afful, F. Sun, M.A. Asadollahi, H. Amiri, A. Abdulkhani, H. Sun, Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective, Front. Bioeng. Biotechnol. 9 (2021) 794304.
M. Cristica, T. Barbaneagra, E. Ciornea, A. Manoliu, Influence of pH on ß-xylanase activity in the filamentous fungi Trichoderma Reesei, Trichoderma Viride and Phanerochaete Chrysosporium, Lucr. Ştiinţifice, Ser. Agron. 55 (2012) 321–325.
P. Held, Enzymatic digestion of polysaccharides, Part II: Optimization of polymer digestion and glucose production in microplates, Biofuel Res. 2013 (2013) 1–5.
A. Salihu, O. Abbas, A.B. Sallau, M.Z. Alam, Agricultural residues for cellulolytic enzyme production by Aspergillus niger: effects of pretreatment, 3 Biotech 5 (2015) 1101–1106.
J.G. Shi, G.M. Zeng, X.Z. Yuan, F. Dai, J. Liu, X.H. Wu, The stimulatory effects of surfactants on composting of waste rich in cellulose, World J. Microbiol. Biotechnol. 22 (2006) 1121–1127.
BPS, Indonesia Sugar Cane Statistics, BPS-Statistic Indones. 14 (2024) 1–108.
L.H. Suryaningrum, Degradasi Lignin pada Ampas Tebu dalam Upaya Pemanfaatannya sebagai Bahan Baku Pakan Ikan, Nucleus 1 (2020) 102–108.
Z. Anwar, M. Gulfraz, M. Irshad, Agro-industrial lignocellulosic biomass a key to unlock the future bio-energy: A brief review, J. Radiat. Res. Appl. Sci. 7 (2014) 163–173.
BPS, Indonesia oil palm statistics, BPS-Statistic Indones. 17 (2024) 1–160.
S.P. Fan, L.Q. Jiang, C.H. Chia, Z. Fang, S. Zakaria, K.L. Chee, High yield production of sugars from deproteinated palm kernel cake under microwave irradiation via dilute sulfuric acid hydrolysis, Bioresour. Technol. 153 (2014) 69–78.
G.W. Lau, P.J.H. King, J.K. Chubo, I.C. King, K.H. Ong, Z. Ismail, T. Robin, I.H. Shamsi, The Potential Benefits of Palm Oil Waste-Derived Compost in Embracing the Circular Economy, Agronomy 14 (2024) 2517.
T.W. Imanisa, E. Mardawati, N. Masruchin, Produksi Enzim Xilanase dari Aspergillus niger melalui Metode Fermentasi Terendam dalam Valorisasi Tandan Kosong Kelapa Sawit sebagai Produk Biorefineri Bernilai Tambah, Biomass, Biorefinery, and Bioeconomy 1 (2023) 14–19.
A.K. Bharti, A. Kumar, A. Kumar, D. Dutt, Wheat bran fermentation for the production of cellulase and xylanase by Aspergillus niger NFCCI 4113, Res. J. Biotechnol. 13 (2018) 11–18.
M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248–254.
F. Rahmawati, R. Basuki, M. Fahri, Y.B. Apriliyanto, T. Kurniadi, V.A. Nareswari, A. Sandri, T. Istiqomah, Reaction Mechanism in Standardized α-Cellulose Content Test: Study from Boehmeria nivea Fiber, Indones. J. Chem. Stud. 3 (2024) 22–27.
W. Geng, R. Narron, X. Jiang, J.J. Pawlak, H. min Chang, S. Park, H. Jameel, R.A. Venditti, The influence of lignin content and structure on hemicellulose alkaline extraction for non-wood and hardwood lignocellulosic biomass, Cellulose 26 (2019) 3219–3230.
V. Elisashvili, E. Kachlishvili, T. Khardziani, S.N. Agathos, Effect of aromatic compounds on the production of laccase and manganese peroxidase by white-rot basidiomycetes, J. Ind. Microbiol. Biotechnol. 37 (2010) 1091–1096.
S. Sánchez-Muñoz, T.R. Balbino, F. de Oliveira, T.M. Rocha, F.G. Barbosa, M.I. Vélez-Mercado, P.R.F. Marcelino, F.A.F. Antunes, E.J.C. Moraes, J.C. dos Santos, S.S. da Silva, S. Sánchez-Muñoz, T.R. Balbino, F. de Oliveira, T.M. Rocha, F.G. Barbosa, M.I. Vélez-Mercado, P.R.F. Marcelino, F.A.F. Antunes, E.J.C. Moraes, J.C. dos Santos, S.S. da Silva, Surfactants, Biosurfactants, and Non-Catalytic Proteins as Key Molecules to Enhance Enzymatic Hydrolysis of Lignocellulosic Biomass, Molecules 27 (2022) 8180.
Y.A. Chen, Y. Zhou, D. Liu, X. Zhao, Y. Qin, Evaluation of the action of Tween 20 non-ionic surfactant during enzymatic hydrolysis of lignocellulose: Pretreatment, hydrolysis conditions and lignin structure, Bioresour. Technol. 269 (2018) 329–338.
Downloads
Published
Issue
Section
License
Copyright (c) 2026 Arif Rahman Hakim, Noor Isnaini Azkiya, Wahyuni Ningsih, Mufid Mufid, Arum Kusuma Wardani, Nisa’ Ulana Al Mukharromah

This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.




