Figures & data
Table 1. Purification of the recombinant β-mannanase from BCC4525.
Fig. 1. Expression of the recombinant MANF3 in KM71 P. pastoris and its characterization. (A) Effect of pH on recombinant BCC4525 β-mannanase activity was determined at different pH values by incubating the enzyme at 70 °C for 10 min in the following buffers; sodium acetate buffer pH 3–6 (closed diamond, 
), sodium phosphate buffer pH 6–8 (open triangle, 
), Tris–HCl buffer pH 8–10 (cross, 
). (B) Effect of temperature on recombinant BCC4525 β-mannanase activity was determined by incubating the enzyme for 10 min at different temperatures. (C) thermal stability test was carried out by incubating the enzyme at 50 °C (closed diamond, ), 60 °C (open square, ), 70 °C (closed triangle, 
), 80 °C (cross, ) or 90 °C (closed circle, 
) for 0.5, 1, 1.5, and 2 h before the remaining activity was assayed. (D) Thermal stability test at 90 °C (closed diamond, ) and 100 °C (open square, ) was carried out for 15–60s.Notes: Values shown are mean ± SD from three independent experiments.
Fig. 2. Hydrolysis of PKM and CM by the recombinant BCC4525 β-mannanase for MOS production. Hydrolysis of PKM (A) and CM (B) was carried out at various time intervals before the reaction products were detected by TLC.
Notes: M1–M6 indicates mannooligosaccharides from mannose to mannohexose. Numbers at the bottom of the graph indicate time of hydrolysis.
Table 2. The amount of released reducing sugarsTable Footnotea from the digesta fluid obtained from in vitro digestibility test.
Supplemental material
