8 research outputs found
Modeling of negative Poisson’s ratio (auxetic) crystalline cellulose Iβ
Energy minimizations for unstretched and stretched cellulose models using an all-atom empirical force field (Molecular Mechanics) have been performed to investigate the mechanism for auxetic (negative Poisson’s ratio) response in crystalline cellulose Iβ from kraft cooked Norway spruce. An initial investigation to identify an appropriate force field led to a study of the structure and elastic constants from models employing the CVFF force field. Negative values of on-axis Poisson’s ratios nu31 and nu13 in the x1-x3 plane containing the chain direction (x3) were realized in energy minimizations employing a stress perpendicular to the hydrogen-bonded cellobiose sheets to simulate swelling in this direction due to the kraft cooking process. Energy minimizations of structural evolution due to stretching along the x3 chain direction of the ‘swollen’ (kraft cooked) model identified chain rotation about the chain axis combined with inextensible secondary bonds as the most likely mechanism for auxetic response
Purification and Characterization of a Low Molecular Weight Endo-xylanase from Mushroom Termitomyces clypeatus
A low molecular weight endo-xylanase (EC 3.2.1.8) was purified from an edible
mushroom Termitomyces clypeatus grown in submerged medium with oat spelt xylan.
Xylanase was purified to apparent homogeneity by ammonium sulfate fractionation and gel
filtration chromatography. Its molecular weight was determined by gel filtration chromatography
and sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be 12 kDa. The
enzyme was found to be most active at 50°C and pH 5.0, being most stable at pH 6.5. The Km
for oat spelt xylan was determined to be 10.4 mg/ml. The specificities of the enzyme was
observed to be highly specific towards oat spelt xylan and was inhibited by mercuric chloride
(HgCl2), N-bromosuccinimide, and trans-1,2-diaminocyclohexane-N′,N′,N′,N′-tetraacetic acid
strongly. The inhibitory action of N-bromosuccinimide on enzyme confirmed the presence of
one tryptophan residue in its substrate-binding site. Amino acid analysis for xylanase showed
the presence of high amount of hydrophobic serine, glycine, threonine, and alanine residues.
The N-terminal sequencing study for the previously purified and characterized 56 kDa
xylanolytic amyloglucosidase reveal the presence of 33.30% identity with glucoamylase chain
A from Aspergillus awamori. The N-terminal sequence analysis of the present 12 kDa enzyme
showed highest similarity (72.22% identity) towards xylanase from Neurospora crassa