First archeointensity results from Portuguese potteries (1550-1750 AD)

Geomagnetic field variations at archeomagnetic timescales can be obtained from well-dated heated structures and archeological potsherds. Here, we present the first archeointensity results obtained oil Portuguese ceramics (1550 to 1750 AD) collected at Brazilian archeological sites. The results are compared to those obtained from `Western Europe and currently available geomagnetic field models. Continuous thermomagnetic and IRM acquisitions curves indicate that Ti-poor titanomagnetite is responsible for the remanence in these ceramic fragments. Five fragments (24 samples) out of twelve analyzed yielded reliable intensity estimates. The row archeointensity data were corrected for TRM anisotropy and cooling rate effect. The mean dipole moments are obtained for three different age intervals: 1550 +/- 30 AD, 1600 +/- 30 AD and 1750 +/- 50 AD. Mean intensities vary from 37.9 +/- 4.2 mu T to 54.8 +/- 7.6 mu T in agreement with the previously reported data for 1550 AD and 1750 AD. Relatively weaker, but still highly dispersed, values were obtained for 1600 AD ceramics.

Functional characterization and oligomerization of a recombinant xyloglucan-specific endo-beta-1,4-glucanase (GH12) from Aspergillus niveus

Xyloglucan is a major structural polysaccharide of the primary (growing) cell wall of higher plants. It consists of a cellulosic backbone (beta-1,4-linked glucosyl residues) that is frequently substituted with side chains. This report describes Aspergillus nidulans strain A773 recombinant secretion of a dimeric xyloglucan-specific endo-beta-1,4-glucanohydrolase (XegA) cloned from Aspergillus niveus. The ORF of the A. niveus xegA gene is comprised of 714 nucleotides, and encodes a 238 amino acid protein with a calculated molecular weight of 23.5 kDa and isoelectric point of 4.38. The optimal pH and temperature were 6.0 and 60 degrees C, respectively. XegA generated a xyloglucan-oligosaccharides (XGOs) pattern similar to that observed for cellulases from family GH12, i.e., demonstrating that its mode of action includes hydrolysis of the glycosidic linkages between glucosyl residues that are not branched with xylose. In contrast to commercial lichenase, mixed linkage beta-glucan (lichenan) was not digested by XegA, indicating that the enzyme did not cleave glucan beta-1,3 or beta-1,6 bonds. The far-UV CD spectrum of the purified enzyme indicated a protein rich in beta-sheet structures as expected for GH12 xyloglucanases. Thermal unfolding studies displayed two transitions with mid-point temperatures of 51.3 degrees C and 81.3 degrees C respectively, and dynamic light scattering studies indicated that the first transition involves a change in oligomeric state from a dimeric to a monomeric form. Since the enzyme is a predominantly a monomer at 60 degrees C. the enzymatic assays demonstrated that XegA is more active in its monomeric state. (c) 2012 Elsevier B.V. All rights reserved.