Xylanase (EC18.104.22.168) is an industrially important enzyme that hydrolyzes xylan by breaking the hemicelluloses of the plant cell wall and produces xylooligosaccharides, xylobiose, and xylose (Beg et al., 2001; Paes et al., 2012). This activity has applications in the food and paper-making industries, along with uses in agriculture and for human health. Recently, interest in xylanase has markedly increased due to its wide utilisation in the food industry such as bread making, the production of corn starch, clarification of fruit juice and wine; animal feeds, and alcoholic fermentation (Kumar et al., 2017; Guido et al., 2019). This enzyme is produced by diverse group of organisms, such as bacteria, algae, and fungi (Collins et al., 2005). However, although xylanase can be obtained from bacteria and yeasts, the enzymes from fungi meet generally industrial demand, since they are usually excreted extracellularly, facilitating extraction from fermentation media (Polizeli et al., 2005).
The diversity of filamentous fungi is extremely high in nature, they have been recognised as a target for screening to find out the appropriate source of enzymes with useful and/or novel characteristics (Quintanilla et al., 2015). They are considered useful producers of xylanase, due to their capability of producing high levels of extracellular enzymes and their very easy cultivability (Shankar et al., 2018). However, improvement of fungal strains for high xylanase production is needed for reducing the cost of the industrial process and also to possess some specialised desirable characteristics.
Genetic engineering, using classical mutation methods and recombinant DNA technology, has been used to increase the expression levels of a large number of microbial enzymes (Adrio & Demain, 2014). However, application of modern techniques to improve the xylanase production does not invalidate the search for wild organisms producing useful enzymes. In addition, due to the need to obtain xylanases with specific processing characteristics, especially in developing countries with low technological capabilities, screening fungal cultures for enzyme production will be suitable. Therefore, screening of naturally occurring fungi may be the best way to obtain new strains and/or xylanases for industrial purposes.
Aspergillus and Penicillium fungi have a saprophytic lifestyle in decaying organic and plant materials; this requires an enzymatic activity that is able to degrade plant cell wall polysaccharides (Tsang et al., 2018). On the other hand, the two plant fungi Cochliobolus sativus ‘foliar pathogen’ and Pyrenophora graminea ‘seed-borne pathogen’ are cereal pathogens that in addition to their role in plant disease, have potential industrial applications; they have been shown to produce cell wall degrading enzymes, including xylanase, during the infection process. These fungi start their lifestyles as biotrophic pathogens degrading plant cell-walls and then switch to necrotrophic growth behaviour (Rodríguez-Decuadro et al., 2014).
In this study, the production of xylanase enzyme from a set of fungi, i.e. Aspergillus, Cochliobolus, Pyrenophora, and Penicillium, covering different lifestyles was compared under submerged culture to determine their potential as sources of industrial enzymes.
The authors wish to express their deep appreciation to the Director General of AECS and the Head of Molecular Biology and Biotechnology Department for their much appreciated help throughout the period of this research.
Thanks are also extended to Dr. A. Al-Daoude for critical reading of the manuscript.
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