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Nanocellulosic-xylan films were prepared employing oat spelt xylan, cellulose whiskers and a plasticizer.
The basic xylanase production medium was prepared at pH 7.0 containing oat spelt xylan.
Relative xylanase activity was determined using 10 mg/ml oat spelt xylan at various pHs.
b The enzyme was incubated at 55 °C with 10 mg/ml oat spelt xylan dissolved in different buffer.
BXA43 was able to release xylose from birchwood xylan, but not from oat spelt xylan or rye arabinoxylan.
The presence of other carbohydrase was analyzed using oat spelt xylan, birchwood xylan, starch, and CMC (10 mg/ml).
Each of the endoxylanases had similar binding activity to wheat flour WU-AX and insoluble oat spelt xylan.
The enzyme showed high specificity towards oat spelt xylan and minute activities were observed with carboxymethyl cellulose and cellobiose.
In contrast, Xyn-C1 exhibited higher binding affinity for oat spelt xylan, but not for birch wood xylan.
The maximum xylanase activity recorded after 2 days of incubation at 37 °C was 20.24 U/ml in the presence of oat spelt xylan.
In this medium, there is a little modification of the main carbon source, the oat spelt xylan was used instead the birchwood xylan (Viet et al. 1991).
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