A refined TALDICE-1a age scale from 55 to 112 ka before present for the Talos Dome ice core based on high-resolution methane measurements

A precise synchronization of different climate records is indispensable for a correct dynamical interpretation of paleoclimatic data. A chronology for the TALDICE ice core from the Ross Sea sector of East Antarctica has recently been presented based on methane synchronization with Greenland and the EDC ice cores and δ18Oice synchronization with EDC in the bottom part (TALDICE-1). Using new high-resolution methane data obtained with a continuous flow analysis technique, we present a refined age scale for the age interval from 55–112 thousand years (ka) before present, where TALDICE is synchronized with EDC. New and more precise tie points reduce the uncertainties of the age scale from up to 1900 yr in TALDICE-1 to below 1100 yr over most of the refined interval and shift the Talos Dome dating to significantly younger ages during the onset of Marine Isotope Stage 3. Thus, discussions of climate dynamics at sub-millennial time scales are now possible back to 110 ka, in particular during the inception of the last ice age. Calcium data of EDC and TALDICE are compared to show the impact of the refinement to the synchronization of the two ice cores not only for the gas but also for the ice age scale.

Enzyme engineering of aminotransferases for improved activity and thermostability

The production by biosynthesis of optically active amino acids and amines satisfies the pharmaceutical industry in its demand for chiral building blocks for the synthesis of various pharmaceuticals. Among several enzymatic methods that allow the synthesis of optically active aminoacids and amines, the use of minotransferase is a promising one due to its broad substrate specificity and no requirement for external cofactor regeneration. The synthesis of chiral compounds by aminotransferases can be done either by asymmetric synthesis starting from keto acids or ketones, and by kinetic resolution starting from racemic aminoacids or amines. The asymmetric synthesis of substituted (S)-aminotetralin, an active pharmaceutical ingredient (API), has shown to have two major factors that contribute to increasing the cost of production. These factors are the raw material cost of biocatalyst used to produce it and product loss during biocatalyst separation. To minimize the cost contribution of biocatalyst and to minimize the loss of product, two routes have been chosen in this research: 1. To engineer the aminotransferase biocatalyst to have greater specific activity, and 2. Improve the engineering of the process by immobilization of biocatalyst in calcium alginate and addition of cosolvents. An (S)-aminotransferase (Mutant CNB03-03) was immobilized, not as purified enzyme but as enzyme within spray dried cells, in calcium alginate beads and used to produce substituted (S)-aminotetralin at 50 °C and pH 7 in experiments where the immobilized biocatalyst was recycled. Initial rate of reaction for cycle 1 (6 hr duration) was determined to be 0.258 mM/min, for cycle 2 (20 hr duration) it decreased by ~50% compared to cycle 1, and for cycle 3 (20 hr duration) it decreased by ~90% compared to cycle 1 (immobilized preparation consisted of 50 mg of spray dried cells per gram of calcium alginate). Conversion to product for each cycle decreased as well, from 100% in cycle 1 (About 50 mM), 80% in cycle 2, and 30% after cycle 3. This mutant was determined to be deactivated at elevated temperatures during the reaction cycle and was not stable enough to allow multiple cycles in its immobilized form. A new mutant aminotransferase was isolated by applying error-prone polymerase chain reaction (PCR) on the gene coding for this enzyme and screening/selection: CNB04-01. This mutant showed a significant improvement in thermostability in comparison to CNB03-03. The new mutant was immobilized and tested under similar reaction conditions. Initial rate remained fairly constant (0.2 mM/min) over four cycles (each cycle with a duration of about 20 hours) with the mutant retaining almost 80% of initial rate in the fourth cycle. The final product concentrations after each cycle did not decrease during recycle experiments. Thermostability of CNB04-01 was much improved compared to CNB03-03. Under the same reaction conditions as stated above, the addition of co-solvents was studied in order to increase substituted tetralone solubility. Toluene and sodium dodecylsulfate (SDS) were used. SDS at 0.01% (w/v) allowed four recycles of the immobilized spray dried cells of CNB04-01, always reaching higher product concentration (80-85 mM) than the system with toluene at 3% (v/v) -70 mM-. The long term activity of immobilized CNB04-01 in a system with SDS 0.01% (w/v) at 50 °C, pH 7 was retained for three cycles (20 to 24 hours each one), reaching always final product concentration between 80-85 mM, but dropping precipitously in the fourth cycle to a final product concentration of 50 mM. Although significant improvement of immobilization on productivity and stability were observed using CNB04-01, another observation demonstrated the limitations of an immobilization strategy on reducing process costs. After analyzing the results of this experiment it was seen that a sudden drop occurred on final product concentration after the third recycle. This was due to product accumulation inside the immobilized preparation. In order to improve the economics of the process, research was focused on developing a free enzyme with an even higher activity, thus reducing raw material cost as well as improving biomass separation. A new enzyme was obtained (CNB05-01) using error-prone PCR and screening using as a template the gene derived from the previous improved enzyme. This mutant was determined to have 1.6 times the initial rate of CNB04-01 and had a higher temperature optimum (55°). This new enzyme would allow reducing enzyme loading in the reaction by five-fold compared to CNB03-03, when using it at concentration of one gram of spray dried cells per liter (completing the reaction after 20-24 hours). Also this mutant would allow reducing process time to 7-8 hours when used at a concentration of 5 grams of spray dried cells per liter compared to 24 hours for CNB03-03, assuming that the observations shown before are scalable. It could be possible to improve the economics of the process by either reducing enzyme concentration or reducing process time, since the production cost of the desired product is primarily a function of both enzyme concentration and process time.

New Data on Welshite, e.g. Ca2Mg3.8Mn0.62+Fe0.12+Sb1.55+O2 [Si2.8Be1.7Fe0.653+Al0.7As0.17O18], an Aenigmatite-Group Mineral

Electron and ion microprobe data on two samples of welshite from the type locality of Langban, Sweden, gave analytical totals of 99.38-99.57 wt.% and BeO contents of 4.82-5.11 wt.%, corresponding to 1.692-1.773 Be/20 O. Mossbauer and optical spectra of one of these samples gave Fe-[iv](3+)/Sigma Fe = 0.91, Fe-[iv](2+)/Sigma Fe = 0.09, and no evidence of Mn3+. The resulting formula for this sample is Ca2Mg3.8Mn0.62+Fe0.12+Sb1.55+O2[Si2.8Be1.7Fe0.653+Al0.7As0.17O18], and that for the second sample, Ca2Mg3.8Mn0.12+Fe0.12+F0.83+Sb1.25+O2[Si2.8Be1.8F0.653+Al0.25As0.25O18], is related by the substitution involving tetrahedral and octahedral sites: 0.59([vi,iv])(Fe,Al)(3+) approximate to 0.42([vi])(Mg,Mn,Fe)(2+) + 0.21(Sb-[vi],As-[iv])(5+), i.e. 3([vi,iv]) M3+ = 2([vi])M(2+) + M-[vi,iv](5+). WelShite is distinctive among aenigmatite-group minerals in the high proportion of Fe 3+ in tetrahedral coordination and is unique in its Be content, substantially exceeding 1Be per formula unit. Given the cation distributions in other minerals related to aenigmatite, we think it is reasonable to assume that at least one tetrahedral site is >50% occupied by Be and that one octahedral site is >50% occupied by Sb, so that welshite should be retained as a distinct species with its own name in the aenigmatite group.

Précis de l'histoire des Hébreux depuis le patriarche Abraham jusqu'en 1840

par L. M. Lambert

Abram : Jugendgeschichte des Erzvaters Abraham nach der talmudischen Sage

von Max Doctor

[Abraham] Geiger's Reform-Judenthum in seinem aufgefundenen Briefwechsel

beleuchtet von einem Freunde des biblischen Judenthums

Rücksprache mit allen Gläubigen des rabbinischen Judenthums über die jüngst erschienene Brochüre betitelt Ansprache an meine Gemeinde von Dr. Abraham Geiger, Breslau 1842

von Israel Deutsch und David Deutsch

Das moderne Judenthum, seiner Emancipation und Reformation entgegen geführt durch die Verdienste Lessings, Moses Mendelssohns und Abraham Geigers : eine historische Charakteristik

von Fredrik Nielsen. Aus d. Dän. übers. von E. Schumacher

Es ist nur ein Gott! : Vertheidigung des jüdischen Volkes zu den Zeiten des Jesus von Nazareth gegen die harten Beschuldigungen der Christen

von Abraham Ben Jaddai. Nach d. 13. engl. Aufl. von Benjamin Wollsteiner