Vegetos
(An International Journal of Plant Research & Biotechnology)
(eISSN: 2229-4473)
Comprehensive evaluation of cell wall degrading enzymes produced by Aspergillus niger under various sucrose concentrations
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Research Articles | Published: 19 May, 2026
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Keywords: n Aspergillus nigern , Cell wall degrading enzymes, Glycosidases, Polygalacturonase, Xylanase
Abstract
The production of cell wall-degrading enzymes by the plant pathogenic fungus Aspergillus niger is of significant interest for both industrial and agriculture applications, particularly in the context of plant pathogenicity and biocontrol strategies. In this study, enzyme production was investigated using Murashige and Skoog (MS) medium supplemented with varying sucrose concentrations (1, 3, and 5%), using sucrose as the sole carbon source. Enzymatic activity was utilized in extracellular, cytoplasmic, and wall-bound fractions, focusing on different enzymes, such as polygalacturonase, xylanase, α/β-galactosidase, and β-glucosidase, for various time periods. Polygalacturonase exhibited the highest enzymatic activity, with peak extracellular activity of 95 U/mL at 72 h in the 3% sucrose condition, followed by a decrease in activity at higher sucrose concentrations. Xylanase activity peaked at 72 h in the 5% sucrose medium, reaching 45 U/mL. Both α-galactosidase and β-glucosidase showed moderate activity, with α-galactosidase reaching 20 U/mL and β-glucosidase 15 U/mL under the 1% sucrose condition. The extracellular fractions consistently displayed the most significant enzyme activity compared to cytoplasmic and wall-bound fractions. Polygalacturonase was determined as the first enzyme generated during the pathogenic process. These findings enhance our understanding of enzyme production dynamics in A. niger and offer insights for industrial and agricultural applications.
References
Annis SL, PH Goodwin (1996) Comparison of cell wall-degrading enzymes produced by highly and weakly virulent isolates of Leptosphaeria maculans in culture. Microbiol Res 151:401–406
Annis SL, PH Goodwin (1997) Recent advances in the molecular genetics of plant cell wall-degrading enzymes produced by plant pathogenic fungi. Eur J Plant Pathol 103:1–14
Bhaskaran S, RH Smith (1993) Carbohydrates, invertase activity, growth and dimorphism in Sporisorium reilianum. Mycopathologia 122:35–41
Fujimori S (2021) Humans have intestinal bacteria that degrade the plant cell walls in herbivores. World J Gastroenterol 27:7784–7791
Houston K, Tucker MR, Chowdhury J, Shirley N, Little A (2016) The plant cell wall: a complex and dynamic structure as revealed by the responses of genes under stress conditions. Front Plant Sci 7:984
Kubicek CP, Starr TL, NL Glass (2014) Plant cell wall–degrading enzymes and their secretion in plant-pathogenic fungi. Ann Rev Phytopathol 52:427–451
Kumar A, Dhiman S, Krishan B, Samtiya M, Kumari A, Pathak N, Kumari A, Aluko RE, Dhewa T (2024) Microbial enzymes and major applications in the food industry: a concise review. Food Prod Process Nutr 6:85
Maldonado MC, Navarro A, DAS Callieri (1986) Production of pectinases by Aspergillus sp using differently pretreated lemon peel as the carbon source. Biotechnol Lett 8:501–504
Mary Wanjiru W, Zhensheng K, H Buchenauer (2002) Importance of cell wall degrading enzymes produced by Fusarium graminearum during infection of wheat heads. Eur J Plant Pathol 108:803–810
Meletiadis J, Meis JFGM, Mouton JW, PE Verweij (2001) Analysis of growth characteristics of filamentous fungi in different nutrient media. J Clin Microbiol 39:478–484
Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426–428
Murray AK, RS Bandurski (1975) Correlative studies of cell wall enzymes and growth. Plant Physiol 56:143–147
Pawar VC, Thaker VS (2006) In vitro efficacy of 75 essential oils against Aspergillus niger. Mycoses 49:316–323
Plassard C, Becquer A, K Garcia (2019) Phosphorus transport in mycorrhiza: How far are we? Trends Plant Sci 24:794–801
Ranwala AP, Suematsu C, H Masuda (1992) The role of β-galactosidases in the modification of cell wall components during muskmelon fruit ripening. Plant Physiol 100:1318–1325
Dos Reis S, Costa MAFRM, Peralta (2003) Xylanase production by a wild strain of Aspergillus nidulans. Acta Sci Biol Sci 25:221–225
Roman-Benn A, Contador CA, Li M-W, Lam H-M, Ah-Hen K, Ulloa PEMC, Ravanal (2023) Pectin: an overview of sources, extraction and applications in food products, biomedical, pharmaceutical and environmental issues. Food Chem Adv 2:100192
Sanghvi GV, Koyani RD, KS Rajput (2010) Thermostable xylanase production and partial purification by solid-state fermentation using agricultural waste wheat straw. Mycology 1:106–112
Santos GB, Á de Sousa Francisco Filho J, Rêgo da Silva Rodrigues R, Rodrigues de Souza (2022) Cellulase production by Aspergillus niger using urban lignocellulosic waste as substrate: evaluation of different cultivation strategies. J Environ Manage 305:114431
Srinivasan R, V Shanmugam (2006) Post-harvest management of black mould rot of onion. Indian Phytopathol 59(3):333–339
Sulyman AO, Igunnu A, SO Malomo (2020) Isolation, purification and characterization of cellulase produced by Aspergillus niger cultured on Arachis hypogaea shells. Heliyon 6:e05668
Thaker VS, Saroop SY, dev Singh (1987) Physiological and biochemical changes associated with cotton fibre development. IV. Glycosidases and β-1,3-glucanase activities. Ann Bot 60:579–585
Tong L, Li Y, Lou X, Wang B, Jin CW Fang (2024) Powerful cell wall biomass degradation enzymatic system from saprotrophic Aspergillus fumigatus. Cell Surf 11:100126
Zhang J, Bruton BD, CL Biles (1999) Fusarium solani endo-polygalacturonase from decayed muskmelon fruit: purification and characterization. Physiol Mol Plant Pathol 54:171–186
van Zyl SRW (2002) Constitutive expression of the Trichoderma reesei β-1,4-xylanase gene (xyn2) and the β-1,4-endoglucanase gene (egI) in Aspergillus niger in molasses and defined glucose media. Appl Microbiol Biotechnol 58:461–468
Author Information
K.M.E Society’s G. M. Momin Women’s College, Bhiwandi, India