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Xylanase plays an important role in the food, feed, and pulp/paper industry. Filamentous fungi have been considered as useful producers of this enzyme from an industrial point of view, due to the fact that they excrete xylanases into the medium. In this study, four fungal species belonging to different genera, i.e. Aspergillus, Cochliobolus, Pyrenophora, and Penicillium were isolated from different sources and compared for their ability to produce xylanase in submerged culture. The fungal species showed enzyme activity as determined by dinitrosalicylic acid (DNS) method. It was found that the two saprophytic Aspergillus strains, i.e A. terreus (Fss 129) and A. niger (SS7) had the highest xylanase activity of 474 and 294 U ml–1 at pH 7 and 8, respectively, in the presence of corn cob hulls after 120 h of incubation. The production of xylanase seemed to be strongly influenced by the interactive effect of initial pH on the fungi. Interestingly, xylanase was better produced by the saprophytic fungi of Aspergillus and Penicillium than by the plant pathogenic ones of Cochliobolus and Pyrenophora. This work provides additional information to support future research on fungi with different lifestyles for food industrial production of xylanase.

Abstract

Xylanase plays an important role in the food, feed, and pulp/paper industry. Filamentous fungi have been considered as useful producers of this enzyme from an industrial point of view, due to the fact that they excrete xylanases into the medium. In this study, four fungal species belonging to different genera, i.e. Aspergillus, Cochliobolus, Pyrenophora, and Penicillium were isolated from different sources and compared for their ability to produce xylanase in submerged culture. The fungal species showed enzyme activity as determined by dinitrosalicylic acid (DNS) method. It was found that the two saprophytic Aspergillus strains, i.e A. terreus (Fss 129) and A. niger (SS7) had the highest xylanase activity of 474 and 294 U ml–1 at pH 7 and 8, respectively, in the presence of corn cob hulls after 120 h of incubation. The production of xylanase seemed to be strongly influenced by the interactive effect of initial pH on the fungi. Interestingly, xylanase was better produced by the saprophytic fungi of Aspergillus and Penicillium than by the plant pathogenic ones of Cochliobolus and Pyrenophora. This work provides additional information to support future research on fungi with different lifestyles for food industrial production of xylanase.

Xylanase (EC3.2.1.8) 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.

1 Materials and methods

1.1 Fungi

Four different fungal species, from the genera Aspergillus, Cochliobolus, Pyrenophora, and Penicillium, were used in this study (Table 1). Two local Aspergillus strains, A. terreus (Fss 129) and A. niger (SS7), isolated from soil by BBAKRI and co-workers (2010), were used. The saprophyte Penicillium canescens strain F58 from the Institute of Plant Biotechnology, Tbilisi, Georgia was also included in the experiments (Assamoi et al. 2008). Two cereal fungal pathogens, Cochliobous sativus (Cs5) and Pyrenophora garminea (Pg16) were chosen in this investigation due to their high virulence and ability to produce cell wall degrading enzymes (Arabi et al. 2004) (Table 1).

Table 1.

Fungal species used in this study

FungiStrainOriginTypeSourceReference
Aspergillus terreus(Fss 129)SyriaSaprobeSoilBakri et al. (2010)
Aspergillus nigerSS7SyriaSaprobeSoilBakri et al. (2010)
Penicillium canescensF58GeorgiaSaprobeSoilAssamoi et al. (2008)
Cochliobolus sativusCs5SyriaPlant pathogenBarley-leavesArabi & Jawhar (2003)
Pyrenophora gramineaPg16SyriaPlant pathogenBarley-seedsArabi et al. (2004)

1.2 Enzyme production

The fungal strains were screened for xylanase production in Erlenmeyer flasks (250 ml) containing 50 ml of basal culture medium (g l–1): yeast extract 5.0; Na2HPO4·2H2O 10.0; KCl 0.5 and MgSO7H2O 0.15. Fresh fungal spores were used as inocula and 1 ml spore suspension (containing around 106 spores ml-1) was added to the sterilised medium and incubated at 30 °C for 5 days in a rotary shaker (120 r.p.m). Xylanase production in the basal medium supplemented with the carbon sources (birchwood xylan, wheat straw, wheat bran, or corncob hulls) was evaluated (Table 2).

Table 2.

The optimal substrate (1%) and temperature for xylanase production by fungal species in submerged culture

FungiSubstrateT (°C)
Aspergillus terreus (Fss 129)Corn cob hulls30
Aspergillus niger (SS7)Corn cob hulls43
Penicillium canescens (F58)Xylan30
Cochliobolus sativus (Cs5)Wheat straw30
Pyrenophora graminea (Pg16)Wheat bran30

1.3 Effect of medium pH and incubation temperature

The influence of initial medium pH on xylanase production was assessed by cultivating the strain in the basal media of pH ranging from 3.0 to 9.0. The effect of temperature was studied by performing the fermentation at different temperatures from 25 to 55 °C.

1.4 Enzyme determination

Xylanase activity was determined by the optimised method described by Bailey and coworkers (1992) using 1% birchwood xylan as substrate. The xylan solution and the enzyme at an appropriate dilution were incubated at 55 °C for 5 min, and the reducing sugars were determined by DNS procedure with xylose as standard (Miller , 1959). The released xylose was measured spectrophotometrically at 540 nm. Xylanase activity was expressed as 1 μmol xylose per min per millilitre (I U ml–1). Results given are the mean of triplicate experiments.

1.5 Statistical analysis

Data was subjected to analysis of variance using the STAT-ITCF statistical programme (2nd version). Differences in xylanase production among different genera were evaluated for significance by using Newman–Keuls test at 5% probability level.

2 Results and discussion

In the current work, xylanase activity of four fungal species belonging to different genera, i.e. Aspergillus, Cochliobolus, Pyrenophora, and Penicillium, was investigated (Table 1). All tested fungi exhibited enzymatic potential, which was highly dependent on the tested species. However, both saprophytic strains A. terreus (Fss 129) and A. niger (SS7) showed maximum xylanase production with corn cob hulls as carbon source (474 and 294 U ml–1, respectively) after 120 h of incubation, followed by the other saprophytic strain Penicillium canescens F58 (54.01 U ml–1) with xylan as a carbon source (Fig. 1).

Fig. 1.
Fig. 1.

Xylanase production by four fungal species in submerged culture media in the presence of corn cob hulls for A. niger and A. terreus, xylan for Penicillium, and wheat straw for both Cochliobolus sativus and Pyrenophora graminea. Error bars display the standard deviation among two biological replicates.

Citation: Acta Alimentaria Acta Alimentaria 49, 2; 10.1556/066.2020.49.2.9

This may reflect their lifestyle mechanisms, since these saprophytic fungi are exposed to complex lignocellulosic materials such as corn cob hulls, and their response is complex and leads to the up-regulated transcription of several carbohydrate active enzymes and accessory proteins (Bakri et al., 2010; Coradetti et al., 2012; Benz et al., 2014). Therefore, this biological lifestyle may help genera Aspergillus to play different functions in soils, which include either active roles, such as the degradation of dead plant material, or inactive roles, where propagules are present in the soil as a resting stage (Arvanitis & Mylonakis, 2015).

On the other hand, the plant pathogens Cochliobolus sativus Cs5 and Pyrenophora graminea Pg16 were the lowest producers of xylanase enzyme (52.81 and 14.26 U ml–1, respectively) with wheat straw as a carbon source (Fig. 1). Although these fungi are widely different in their infection behaviour as foliar and seed borne pathogens, however, they started their lifestyles as biotrophs for penetrating plant cell walls and intimate contact with living host plant cell membranes, and then for the necrotrophic stage the fungus can produce a full range of digestive enzymes, and a complete expression of digestive metabolism, so that the fungus can take full advantage of the plant cell as a nutrient source (Jobic et., al 2007). Interestingly, our data demonstrated that the seed-borne pathogen Pyrenophora graminea produced lower amounts of xylanase enzyme than the foliar Cochliobolus sativus; this might be attributed to the foliar infection occurring faster than seed infection, which requires more enzymes for degrading the plant cell wall and consequently spreading the mycelium very fast.

Temperature and pH are important cultural parameters that determine growth rate and have major effect on levels of enzyme production by microorganisms. Fungal xylanases generally exhibit activity within a broad pH range, i.e. pH 3 to pH 8 (Subramaniyan & Prema, 2002). The same is true for this study, with all fungal species exhibiting xylanase activities across pH 4–8 (Fig. 2). Our results showed that the optimum pH for xylanase production was between 7 and 8 for the genus Aspergillus, whereas, it ranged from 4.5 to 6.5 for the other fungi (Fig. 2). These observations concurred with earlier generalisations that fungal xylanases are more stable at acidic to neutral pH than at basic pH (Collins et al., 2005).

Fig. 2.
Fig. 2.

Effect of different initial pH values on xylanase production by four fungal species

: A. terreus; : A. niger; : P. canescens; : C. sativus; : P. graminea

Citation: Acta Alimentaria Acta Alimentaria 49, 2; 10.1556/066.2020.49.2.9

The fermentation temperature has marked effect on the level of xylanase production, as it plays important role in the metabolic activities of microorganisms (Seyis & Aksoz, 2003). In this study, the optimum temperature of 30 °C (except for A. niger it was 43 °C) was observed for xylanase production for the fungal species (Fig. 3; Table 2). However, a decrease in xylanase production was observed at 25 °C, and increasing the incubation temperature up to 55 °C significantly reduced enzyme production (Fig. 3). This decline is due to the lower growth rate of fungi at high temperature. The high and low incubation temperatures cause the inhibition of fungal growth that ultimately leads to the decline in enzyme synthesis (Lenartovicz et al., 2003). On the other hand, submerged culture was used in this study, which allows control over the degree of aeration, pH and temperature of the medium, as well as control over other environmental factors required for optimum growth of organisms (Escobar et., al 2017).

Fig. 3.
Fig. 3.

Effect of temperature on xylanase production by four fungal species

: A. terreus; : A. niger;: P. canescens;: C. sativus;:P. graminea

Citation: Acta Alimentaria Acta Alimentaria 49, 2; 10.1556/066.2020.49.2.9

3 Conclusions

Our study revealed significant differences in xylanase production found among the four different genera, i.e. Aspergillus, Cochliobolus, Pyrenophora, and Penicillium in liquid medium. Interestingly, xylanase was produced better by the saprophytic strains of Aspergillus and Penicillium than by the plant pathogenic ones of Cochliobolus and Pyrenophora. It was found that the two saprophytic Aspergillus strains, A. terreus (Fss 129) and A. niger (SS7), had the highest xylanase activity of 474 and 294 U ml–1 at pH 7 and 8, respectively. Additionally, data showed that the production of xylanase seemed to be strongly influenced by the interactive effect of initial pH on the fungi. The optimum pH for xylanase production by both isolates was found betxween 7 and 8 for the genus Aspergillus, whereas from 4.5 to 6.5 for others at 30 and 43 °C.

*

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.

References

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  • Arvanitis, M. & Mylonakis, E. (2015): Diagnosis of invasive aspergillosis: recent developments and ongoing challenges. Eur. J. Clin. Invest., 45, 646-652

    • Search Google Scholar
    • Export Citation
  • Assamoi, A.A., Delvigne, F., Aldric, J.M., Destain, J. & Thonart, P. (2008): Improvement of xylanase production by Penicillium canescens 10-10c in solid-state fermentation. Biotech., Agron., Soci. Envir., 12, 111-118

    • Search Google Scholar
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    • Search Google Scholar
    • Export Citation
  • Bakri, Y., Masson, M. & Thonart, P. (2010): Isolation and identification of two new fungal strains for xylanase production. Appl. Bioch. Biotech., 162, 1626-1634

    • Search Google Scholar
    • Export Citation
  • Beg, Q.K., Kapoor, M., Mahajan, L. & Hoondal, G.S. (2001): Microbial xylanases and their industrial applications: a review. Appl. Microb. Biotech., 56, 326-338

    • Search Google Scholar
    • Export Citation
  • Benz, J.P., Chau, B.H., Zheng, D., Bauer, S., Glass, N.L. & Somervtlle, C.R. (2014): A comparative systems analysis of polysaccharide-elicited responses in Neurospora crassa reveals carbon source-specific cellular adaptations. Mol Microb., 91 275-299

    • Search Google Scholar
    • Export Citation
  • Collins, T., Gerday, C. & Feller, G. (2005): Xylanases, xylanase families and extremophilic xylanases. FEMS Microb. Rev., 29 3-23

  • Coradetti, S.T., Craig, J.P., Xiong, Y., Shock, T., Tian, C. & Glass, N.L. (2012): Conserved and essential transcription factors for cellulase gene expression in ascomycete fungi. Proceedings of the National Academy of Sciences, USA, 109: 7397-7402

    • Search Google Scholar
    • Export Citation
  • Escobar, L.M.A., López, Y.G. & Restrepo, S.U. (2017): Effects of aeration, agitation and pH on the production of mycelial biomass and exopolysaccharide from the filamentous fungus Ganoderma lucidum. Dyna, 84, 72-79

    • Search Google Scholar
    • Export Citation
  • Guido, E.S., Silveira, J.T. & Kalil, S.J. (2019): Enzymatic production of xylooligosaccharides from beechwood xylan: effect of xylanase preparation on carbohydrate profile of the hydrolysates. Int. Food Res. J. ,26 713-721

    • Search Google Scholar
    • Export Citation
  • Jobic, C., Boisson, A.M., Gout, E., Rascle, C., Fevre, M., … & Bligny, R. (2007): Metabolic processes and carbon nutrient exchanges between host and pathogen sustain the disease development during sunflower infection by Sclerotinia sclerotiorum. Planta, 226, 251-265

    • Search Google Scholar
    • Export Citation
  • Kumar, D., Kumar, S.S., Kumar, J., Kumar, O., Mishra, S.V., … & Malyan, S.K. (2017): Xylanases and their industrial applications: A review. Biochem. Cell. Arch., 17, 353-360

    • Search Google Scholar
    • Export Citation
  • Lenartovicz, V., Marques De Souza, C.G., Guillen Moreira, F. & Peralta, R.M. (2003): Temperature and carbon source affect the production and secretion of a thermostable β-xylosidase by Aspergillus fumigates. Process Biochem., 38, 1775-1780

    • Search Google Scholar
    • Export Citation
  • Miller, L. (1959): Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem., 31, 426-428

  • Paes, G., Berrin, J.G. & Beaugrand, J. (2012): GH11 xylanases: structure/function/properties relationships and applications. Biotech. Adv., 30, 564-592

    • Search Google Scholar
    • Export Citation
  • Polizell, M.L.T.M., Rizzatti, A.C.S., Monti, R., Terenzi, H.F., Jorge, J.A. & Amorim, D.S. (2005): Xylanases from fungi: properties and industrial applications. Appl Microb. Biotech., 67, 577-591

    • Search Google Scholar
    • Export Citation
  • Quintanilla, D., Hagemann, T., Hansen, K. & Gernaey, K.V. (2015): Fungal morphology in industrial enzyme production-Modelling and monitoring. -in: Krull, R. & Bley, T. (Eds) Filaments in Bioprocesses. Adv. Biochem. Eng. Biotechnol., 149, 29-54

    • Search Google Scholar
    • Export Citation
  • Rodríguez-Decuadro, S., Silva, P., Bentancur, O., Gamba, F. & Pritsch, C. (2014): Histochemical characterization of early response to Cochliobolus sativus infection in selected barley genotypes. Phytopathology, 104, 715-723

    • Search Google Scholar
    • Export Citation
  • Shankar, T., Harinathan, B., Palpperumal, S., Sankaralingam, S. & Jamunadevi, B. (2018): Biodiversity of xylanase producing fungi present in the leaf litter soil of Munnar Hills, Kerala. Res. J. Life Sci. Bio., Pharm. Chem. Sci., 4, 37

    • Search Google Scholar
    • Export Citation
  • Seyis, I. & Aksoz, N. (2003): Determination of some physiological factors affecting xylanase production from Trichodenna harzianuml073-d3. New Microb., 26, 75-81

    • Search Google Scholar
    • Export Citation
  • Subramaniyan, S. & Prema, P. (2002): Biotechnology of microbial xylanases: enzymology, molecular biology and application. Crit. Rev. Biotechnol., 22, 33-46

    • Search Google Scholar
    • Export Citation
  • Tsang, C.C., Tang, J.Y.M., Lau, S.K.P. & Woo, P.C.Y. (2018): Taxonomy and evolution of Aspergillus, Penicillium and Talaromyces in the omics era – Past, present and future. Comput. Struct. Biotech. J., 16, 197-210

    • Search Google Scholar
    • Export Citation

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  • Adrio, J.L. & Demain, A.L. (2014): Microbial enzymes: tools for biotechnological processes. Biomolecules, 4, 117-139

  • Arabi, M.I.E. & Jawhar, M. (2003): Pathotypes of spot blotch (Cochliobolus safivus) on barley in Syria. J. Plant Pathol., 85, 193-196

  • Arabi, M.I.E., Jawhar, M., Al-Safadi, B. & Mirali, N. (2004): Yield response of barley to leaf stripe (Pyrenophora graminea) under experimental conditions in southern Syria. J. Phytopathol., 152, 519-523

    • Search Google Scholar
    • Export Citation
  • Arvanitis, M. & Mylonakis, E. (2015): Diagnosis of invasive aspergillosis: recent developments and ongoing challenges. Eur. J. Clin. Invest., 45, 646-652

    • Search Google Scholar
    • Export Citation
  • Assamoi, A.A., Delvigne, F., Aldric, J.M., Destain, J. & Thonart, P. (2008): Improvement of xylanase production by Penicillium canescens 10-10c in solid-state fermentation. Biotech., Agron., Soci. Envir., 12, 111-118

    • Search Google Scholar
    • Export Citation
  • Bailey, M.J., Bailey, P. & Poutanen, R. (1992): Interlaboratory testing of methods for assay of xylanase activity. J. Biotechnol., 23, 257-270

    • Search Google Scholar
    • Export Citation
  • Bakri, Y., Masson, M. & Thonart, P. (2010): Isolation and identification of two new fungal strains for xylanase production. Appl. Bioch. Biotech., 162, 1626-1634

    • Search Google Scholar
    • Export Citation
  • Beg, Q.K., Kapoor, M., Mahajan, L. & Hoondal, G.S. (2001): Microbial xylanases and their industrial applications: a review. Appl. Microb. Biotech., 56, 326-338

    • Search Google Scholar
    • Export Citation
  • Benz, J.P., Chau, B.H., Zheng, D., Bauer, S., Glass, N.L. & Somervtlle, C.R. (2014): A comparative systems analysis of polysaccharide-elicited responses in Neurospora crassa reveals carbon source-specific cellular adaptations. Mol Microb., 91 275-299

    • Search Google Scholar
    • Export Citation
  • Collins, T., Gerday, C. & Feller, G. (2005): Xylanases, xylanase families and extremophilic xylanases. FEMS Microb. Rev., 29 3-23

  • Coradetti, S.T., Craig, J.P., Xiong, Y., Shock, T., Tian, C. & Glass, N.L. (2012): Conserved and essential transcription factors for cellulase gene expression in ascomycete fungi. Proceedings of the National Academy of Sciences, USA, 109: 7397-7402

    • Search Google Scholar
    • Export Citation
  • Escobar, L.M.A., López, Y.G. & Restrepo, S.U. (2017): Effects of aeration, agitation and pH on the production of mycelial biomass and exopolysaccharide from the filamentous fungus Ganoderma lucidum. Dyna, 84, 72-79

    • Search Google Scholar
    • Export Citation
  • Guido, E.S., Silveira, J.T. & Kalil, S.J. (2019): Enzymatic production of xylooligosaccharides from beechwood xylan: effect of xylanase preparation on carbohydrate profile of the hydrolysates. Int. Food Res. J. ,26 713-721

    • Search Google Scholar
    • Export Citation
  • Jobic, C., Boisson, A.M., Gout, E., Rascle, C., Fevre, M., … & Bligny, R. (2007): Metabolic processes and carbon nutrient exchanges between host and pathogen sustain the disease development during sunflower infection by Sclerotinia sclerotiorum. Planta, 226, 251-265

    • Search Google Scholar
    • Export Citation
  • Kumar, D., Kumar, S.S., Kumar, J., Kumar, O., Mishra, S.V., … & Malyan, S.K. (2017): Xylanases and their industrial applications: A review. Biochem. Cell. Arch., 17, 353-360

    • Search Google Scholar
    • Export Citation
  • Lenartovicz, V., Marques De Souza, C.G., Guillen Moreira, F. & Peralta, R.M. (2003): Temperature and carbon source affect the production and secretion of a thermostable β-xylosidase by Aspergillus fumigates. Process Biochem., 38, 1775-1780

    • Search Google Scholar
    • Export Citation
  • Miller, L. (1959): Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem., 31, 426-428

  • Paes, G., Berrin, J.G. & Beaugrand, J. (2012): GH11 xylanases: structure/function/properties relationships and applications. Biotech. Adv., 30, 564-592

    • Search Google Scholar
    • Export Citation
  • Polizell, M.L.T.M., Rizzatti, A.C.S., Monti, R., Terenzi, H.F., Jorge, J.A. & Amorim, D.S. (2005): Xylanases from fungi: properties and industrial applications. Appl Microb. Biotech., 67, 577-591

    • Search Google Scholar
    • Export Citation
  • Quintanilla, D., Hagemann, T., Hansen, K. & Gernaey, K.V. (2015): Fungal morphology in industrial enzyme production-Modelling and monitoring. -in: Krull, R. & Bley, T. (Eds) Filaments in Bioprocesses. Adv. Biochem. Eng. Biotechnol., 149, 29-54

    • Search Google Scholar
    • Export Citation
  • Rodríguez-Decuadro, S., Silva, P., Bentancur, O., Gamba, F. & Pritsch, C. (2014): Histochemical characterization of early response to Cochliobolus sativus infection in selected barley genotypes. Phytopathology, 104, 715-723

    • Search Google Scholar
    • Export Citation
  • Shankar, T., Harinathan, B., Palpperumal, S., Sankaralingam, S. & Jamunadevi, B. (2018): Biodiversity of xylanase producing fungi present in the leaf litter soil of Munnar Hills, Kerala. Res. J. Life Sci. Bio., Pharm. Chem. Sci., 4, 37

    • Search Google Scholar
    • Export Citation
  • Seyis, I. & Aksoz, N. (2003): Determination of some physiological factors affecting xylanase production from Trichodenna harzianuml073-d3. New Microb., 26, 75-81

    • Search Google Scholar
    • Export Citation
  • Subramaniyan, S. & Prema, P. (2002): Biotechnology of microbial xylanases: enzymology, molecular biology and application. Crit. Rev. Biotechnol., 22, 33-46

    • Search Google Scholar
    • Export Citation
  • Tsang, C.C., Tang, J.Y.M., Lau, S.K.P. & Woo, P.C.Y. (2018): Taxonomy and evolution of Aspergillus, Penicillium and Talaromyces in the omics era – Past, present and future. Comput. Struct. Biotech. J., 16, 197-210

    • Search Google Scholar
    • Export Citation

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Co-editor(s): A. Halász

       Editorial Board

L. Abrankó (Budapest), J. Baranyi (Norwich), I. Bata-Vidács (Budapest), J. Beczner (Budapest), Gy. Biró (Budapest), A. Blázovics (Budapest), F. Capozzi (Bologna), M. Carcea (Rome), Zs. Cserhalmi (Budapest), M. Dalla Rosa (Bologna), I. Dalmadi (Budapest), K. Demnerova (Prague), Muying Du (Chongqing), S. N. El (Izmir), S. B. Engelsen (Copenhagen), E. Gelencsér (Budapest), V. M. Gómez-López (Murcia), J. Hardi (Osijek), N. Ilić (Novi Sad), D. Knorr (Berlin), H. Köksel (Ankara), R. Lásztity (Budapest), K. Liburdi (Cork), M. Lindhauer (Detmold), M.-T. Liong (Penang), M. Manley (Stellenbosch), M. Mézes (Gödöllő), Á. Németh (Budapest), Q. D. Nguyen (Budapest), L. Nyström (Zürich), V. Piironen (Helsinki), M. Rychtera (Prague), K. Scherf (München), R. Schönlechner (Wien), A. Sharma (Mumbai), A. Szarka (Budapest), M. Szeitzné Szabó (Budapest), L. Varga (Mosonmagyaróvár), R. Venskutonis (Kaunas), B. Wróblewska (Olsztyn)

 

Acta Alimentaria
Central Food Research Institute
Herman Ottó út 15.
H-1022 Budapest, Hungary
Phone: (36 1) 356 4673 or 355 8244 ext. 179
Fax: (36 1) 356 4673
E-mail: actaalim@cfri.hu

The author instruction is available in PDF.
Please, download the file from HERE.

  

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