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Fig. 7 | Biotechnology for Biofuels

Fig. 7

From: The Coptotermes gestroi aldo–keto reductase: a multipurpose enzyme for biorefinery applications

Fig. 7

Effects of H2O2 generation during BG hydrolysis and hydrolytic synergy of enzymatic cocktails and CgAKR-1. a One hundred nanograms of each enzyme (CgGH9, CgAKR-1, and a commercial catalase), NADPH, and 1.0% BG were used in the assays (Mix). The reaction was carried out at 30 °C for 1, 14, or 24 h. The DS was calculated as follows: (g/L) of reducing sugar of (CgGH9 + enzyme)/(g/L) of reducing sugars of CgGH9. No hydrolysis was detected by CgAKR-1 in the absence of CgGH9. b Celluclast was used for hydrolysis at 10 FPU/g of raw sugarcane bagasse (SCB) or phosphoric acid-pretreated sugarcane bagasse (PASB) and (0.5 mg of CgAKR-1 plus NADPH)/g sugarcane bagasse. The reactions were performed at pH 5.7 for 2, 6, or 24 h at 30 °C and 1000 rpm. The degree of synergism (DS) was calculated as follows: g/L released sugar (Celluclast plus CgAKR-1)/g/L released sugar (Celluclast). Denatured CgAKR-1 was used as the control for all substrates. No hydrolysis was detected by CgAKR-1/NAPDH in the absence of Celluclast

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