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. 2005 Jul;71(7):3504–3511. doi: 10.1128/AEM.71.7.3504-3511.2005

TABLE 6.

Sequential reactions against CAX by XynA and EngL attached to mini-CbpAa

Added enzyme(s)
Liberated reducing sugar (μM) Synergy
In first reaction (time of reaction) In second reaction (time of reaction)
XynA-mini-CbpA1&2 (15 h) EngL-mini-CbpA1&2 (5 h) 108 (5.0) 1.4
EngL-mini-CbpA1&2 (15 h) XynA-mini-CbpA1&2 (5 h) 97 (2.1) 1.1
XynA-mini-CbpA5&6 (15 h) EngL-mini-CbpA5&6 (5 h) 163 (0.9) 1.3
EngL-mini-CbpA5&6 (15 h) XynA-mini-CbpA5&6 (5 h) 144 (1.1) 1
Control reactions
    XynA-mini-CbpA1&2 (5 h) 24 (2.0)
    XynA-mini-CbpA1&2 (20 h) 24 (1.0)
    XynA-mini-CbpA5&6 (5 h) 19 (0.3)
    XynA-mini-CbpA5&6 (20 h) 21 (0.4)
    EngL-mini-CbpA1&2 (5 h) 52 (1.7)
    EngL-mini-CbpA1&2 (20 h) 60 (0.9)
    EngL-mini-CbpA5&6 (5 h) 105 (2.0)
    EngL-mini-CbpA5&6 (20 h) 134 (3.7)
a

CAX (0.5%) was degraded by 0.1 μM EngL and XynA at 37°C for 20 h. Mini-scaffolding proteins (mini-CbpA1&2 or mini-CbpA5&6) were at 0.1 μM. The second enzyme was added immediately after the end of the incubation period of the first reaction. The number in parentheses indicates standard deviation.