Dataset on optimization of lignin peroxidase production by Endomelanconiopsis sp. under submerged fermentation using one factor at a time approach

Abstract

One factor at a time approach was employed for the optimization of media components, physical factors and additional additives for lignin peroxidase (LiP) production under submerged fermentation by the endophytic fungus Endomelanconiopsis sp. The optimized conditions derived were: carbon source (dextrose 10 g/L), nitrogen source (ammonium tartarate 0.027 g/L), veratryl alcohol (1 mM), MnSO₄ (0.5 g/L), inoculum concentration (3 mycelial plugs), pH (5), temperature (30 °C) and Tween 80 (1.5%). A 40 fold increase of enzyme activity was observed after the single parameter optimization. The lignin peroxidase (LiP) production to the level of 345.26 ± 0.52 IU/mL indicates that the fungus has the commercial potential for LiP.

Specifications Table

Subject area	Biotechnology
More specific subject area	Bioprocess technology- enzyme production
Type of data	Figure
How data was acquired	UV–Vis spectrophotometric assay
Data format	Raw
Parameters for data collection	Supernatants were withdrawn periodically as per factor analyzed
Description of data collection	LiP production by the strain was optimized by one factor at a time method under submerged fermentation. LiP activity after each experiment was measured by veratryl alcohol oxidation at 310 nm [2]
Data source location	Plant Biotechnology Laboratory, Department of Biotechnology, Cochin University of Science and Technology, Kerala, India.
Data accessibility	Data is with this article

Value of the Data •The data provided the optimum condition required for the production of lignin peroxidase from Endomelanconiopsis sp. •The data would be valuable to the researchers who work on optimization of different factors for LiP production from endophytic ascomycetes. •This achieved a yield of maximum enzyme activity under the optimized conditions presented in the article.

1. Data

The data presented in the article provides information on the optimization of various factors that influence the lignin peroxidase (LiP) production from Endomelanconiopsis sp. under submerged fermentation system using one factor at a time method. The article includes the single parameter optimization of media components (Fig. 1, Fig. 2, Fig. 3 a and b) (Supplementary Tables 1, 2, 3a, and b), physical factors (Fig 3 c–e) (Supplementary Tables 3c–e) and additional additives (Fig. 4) (Supplementary Table 4) by varying single factor at a time and keeping all the others constant. After the optimization of enzyme production, time course analysis (Fig. 5) (Supplementary Table 5) provided a maximum activity of 345.26 ± 0.52 IU/mL using 3 mycelial plugs as inoculum concentration at pH 5 with an incubation temperature of 30 °C.

Fig. 1.

Effect of carbon source (dextrose) on LiP production from Endomelanconiopsis sp.

Fig. 2.

Effect of nitrogen source (ammonium tartarate) on LiP production from Endomelanconiopsis sp.

Fig. 3.

Effect of various factors on LiP production from Endomelanconiopsis sp.: a) veratryl alcohol, b) MnSO₄, c) inoculum concentration d) pH, e) temperature.

Fig. 4.

Effect of various factors on LiP production from Endomelanconiopsis sp.: a) detergents, b) tween 80.

Fig. 5.

Time course analysis under optimized condition for LiP production.

2. Experimental design, materials and methods

Single parameter optimization was used to assess the effect of each factor on LiP production from Endomelanconiopsis sp. under submerged fermentation. The medium selected for submerged fermentation was modified Tien and Kirk medium [3] modified to omit aluminium potassium sulphate (AlK(SO₄)₂·12H₂O) and nitriloacetate. The various factors selected were carbon source (dextrose 2–20g/L), nitrogen source (ammonium tartarate 0–0.88g/L), inducer concentration (0.5–6mM veratryl alcohol), MnSO₄ concentration (0–1.5g/L), inoculum concentration (1–6 mycelial plugs), pH (2–7), temperature (20–40 °C) and detergents at 1% concentration (CTAB, SDS, Triton X, Tween 80 and Tween 20). LiP activity was determined by H₂O₂ dependent oxidation of veratryl alcohol at 310 nm [2] using spectrophotometer (Shimadzu UV 1800) and the enzyme activity was expressed in IU/mL. An International Unit (IU) is defined as the amount of enzyme activity which will catalyze the transformation of 1 μmol of the substrate per minute under standard conditions. Protеin contеnt was determinеd by Lowry's mеthod [1] using bovine serum albumin as standard and the specific activity was expressed as IU/mg. A time course analysis was conducted with all the factors at optimum conditions. All the experiments were done in triplicates and the data were graphically plotted using Graph Pad prism version 6.01.

Authors' contribution

NP participated in the design of experiments, submerged fermentation experiments, optimization, and drafted the revised manuscript. AC and ACK participated in helping submerged fermentation optimization. PN conceived of the experiment, coordinated the work and carefully revised the manuscript. All the authors read and approved the manuscript.

Conflict of Interest

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Appendix A. Supplementary data

The following are the Supplementary data to this article: