Determining the rp-process flow through 56Ni: resonances in 57Cu(p,γ)58Zn identified with GRETINA.

An approach is presented to experimentally constrain previously unreachable (p, γ) reaction rates on nuclei far from stability in the astrophysical rp process. Energies of all critical resonances in the (57)Cu(p,γ)(58)Zn reaction are deduced by populating states in (58)Zn with a (d, n) reaction in inverse kinematics at 75 MeV/u, and detecting γ-ray-recoil coincidences with the state-of-the-art γ-ray tracking array GRETINA and the S800 spectrograph at the National Superconducting Cyclotron Laboratory. The results reduce the uncertainty in the (57)Cu(p,γ) reaction rate by several orders of magnitude. The effective lifetime of (56)Ni, an important waiting point in the rp process in x-ray bursts, can now be determined entirely from experimentally constrained reaction rates.

Low-energy enhancement in the photon strength of 95Mo.

A new experimental technique is presented using proton-γ-γ correlations from (94)Mo(d,p)(95)Mo reactions which allows for the model-independent extraction of the photon strength function at various excitation energies using primary γ-ray decay from the quasicontinuum to individual low-lying levels. Detected particle energies provide the entrance excitation energies into the residual nucleus while γ-ray transitions from low-lying levels specify the discrete states being fed. Results strongly support the existence of the previously reported low-energy enhancement in the photon strength function.

Superdeformation in the N = Z nucleus 36Ar: experimental, deformed mean field, and spherical shell model descriptions

A superdeformed rotational band has been identified in 36Ar, linked to known low-spin states, and observed to its high-spin termination at Ipi = 16(+). Cranked Nilsson-Strutinsky and spherical shell model calculations assign the band to a configuration in which four pf-shell orbitals are occupied, leading to a low-spin deformation beta(2) approximately 0.45. Two major shells are active for both protons and neutrons, yet the valence space remains small enough to be confronted with the shell model. This band thus provides an ideal case to study the microscopic structure of collective rotational motion.

Enzyme analyses demonstrate that beta-methylbutyric acid is converted to beta-hydroxy-beta-methylbutyric acid via the leucine catabolic pathway by galactomyces reessii

Galactomyces reessii accomplishes the enzymatic transformation of beta-methylbutyric acid (isovaleric acid) to beta-hydroxy-beta-methylbutyric acid. The enzymatic basis for this bioconversion was evaluated by analyzing cell-free extracts of G. reessii for enzyme activities commonly associated with leucine catabolism. G. reessii extracts contained activities for acyl-CoA synthetase, acyl-CoA dehydrogenase, and enoyl-CoA hydratase, whereas beta-methylbutyric acid hydroxylase, alpha-ketoisocaproate oxygenase, and acyl-CoA oxidase (with isovaleryl-CoA as substrate) were not observed. Furthermore, beta-methylbutyric acid is initially activated to isovaleryl-CoA by acyl-CoA synthetase, dehydrogenated to methylcrotonyl-CoA by acyl-CoA dehydrogenase, hydrated to beta-hydroxy-beta-methylbutyric acid-CoA by enoyl-CoA hydratase, and hydrolyzed to beta-hydroxy-beta-methylbutyric acid in G. reessii extracts. Cell-free extracts converted both isovaleryl-CoA and methylcrotonyl-CoA into beta-hydroxy-beta-methylbutyric acid, thus demonstrating that beta-methylbutyric acid is part of the leucine catabolic pathway. The rate of beta-methylbutyric acid conversion to beta-hydroxy-beta-methylbutyric acid with cell-free extract was 0. 013 &mgr;mol beta-hydroxy-beta-methylbutyric acid (mg protein)-1 h-1, while the conversion rate of leucine was fivefold lower. With whole cells, the highest production rate [0.042 &mgr;mol beta-hydroxy-beta-methylbutyric acid (g cells)-1 h-1] was also observed with beta-methylbutyric acid. The results indicate that beta-methylbutyric acid is transformed to beta-hydroxy-beta-methylbutyric acid through the leucine catabolic pathway.

Optimal pH control of batch processes for production of curdlan by Agrobacterium species.

We sought an optimal pH profile to maximize curdlan production in a batch fermentation of Agrobacterium species. The optimal pH profile was calculated using a gradient iteration algorithm based on the minimum principle of Pontryagin. The model equations describing cell growth and curdlan production were developed as functions of pH, sucrose concentration, and ammonium concentration, since the specific rates of cell growth and curdlan production were highly influenced by those parameters. The pH profile provided the strategy to shift the culture pH from the optimal growth condition (pH 7.0) to the optimal production one (pH 5.5) at the time of ammonium exhaustion. By applying the optimal pH profile in the batch process, we obtained significant improvement in curdlan production (64 g L-1) compared to that of constant pH operation (36 g L-1).