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Biochemistry & Molecular Biology

Characterization of cellulolytic enzyme system of Schizophyllum commune mutant and evaluation of its efficiency on biomass hydrolysis

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Pages 1289-1299 | Received 09 Jun 2016, Accepted 17 Mar 2017, Published online: 10 May 2017

Figures & data

Table 1. Cellulose, hemicellulose, and lignin content of native and alkaline pretreated lignocellulosic biomass.

Table 2. Comparison of cellulolytic and hemicellulolytic enzyme activities between the parental strain S. commune BCC23363 and mutant strain G-135 cultivated on Avicel-PH101 (n = 4).

Table 3. Lignocellulose-degrading enzyme production by S. commune G-135 cultivated on different carbon sources (n = 4).

Fig. 1. Effects of temperature (A) and pH (B) on composite enzyme activities produced by S. commune G-135.

Notes: Reactions contained 1% (w/v) CMC, 5% (w/v) filter paper, 1% (w/v) Birchwood xylan, 0.5% (w/v) LBG, 0.1%(w/v) p-nitrophenyl-β-D-glucopyranoside, and0.1% (w/v) p-nitrophenyl-β-D-xylopyranoside as the substrates for CMCase, FPase, xylanase, mannanase, β-glucosidase, and β-xylosidase, respectively. The optimal temperature was determined at pH 5.0 in 100 mM sodium acetate buffer at varying temperatures. The optimal pH was determined by incubating enzyme with substrates in 100 mM citrate buffer (pH 2–4), sodium acetate buffer (pH 4–6), 100 mM sodium phosphate buffer (pH 6–8), and 100 mM Tris-HCl buffer (pH 8–10) at 50 °C. Relative activity was based on the enzyme activity at optimal temperature and pH of CMCase (50.8 U/mL), FPase (0.6 U/mL), xylanase (1145 U/mL), mannanase (12.0 U/mL), β-glucosidase (8.0 U /mL), and β-xylosidase (0.015 U/mL). Averaged data from triplicate samples are reported (n = 3).
Fig. 1. Effects of temperature (A) and pH (B) on composite enzyme activities produced by S. commune G-135.

Fig. 2. Conversion efficiency of different pretreated agricultural biomass using SC-Cel and effects of downstream enzyme supplementation.

Notes: Reactions contained 5% (w/v) biomass in 50 mM sodium acetate buffer, pH 5.0 with a varying dosage of SC-Cel produced on Avicel-PH101 as the carbon source (SC-Cel) in the absence or presence of the extra β-xylosidase (BX) at an enzyme loading of 2 U/g biomass. (A) % glucose recovery (B) % xylose recovery. Averaged data from triplicate samples are reported (n = 3).
Fig. 2. Conversion efficiency of different pretreated agricultural biomass using SC-Cel and effects of downstream enzyme supplementation.

Table 4. Summary of peptide identified in S. commune G-135 secretome.

Table 5. The reducing sugar release from the hydrolysis of various biomass at the enzyme dosage of 2, 4, and 6 FPU/g biomass (n = 3)

Supplemental material

TBBB_1320937_Supplemental_Material.docx

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