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We have studied the percolation limit of synthetic ferrimagnetic media (SFM) by the measurement of noise power and third harmonic ratio and by imaging with a high-resolution magnetic force microscope (MFM). The noise power spectrum, which helps to find the onset of percolation, is significantly different in SFM structures compared to the conventional recording media. Properties of the stabilization layers, such as switching field distribution (SFD), are highly influential in deciding the integrated noise power spectrum. With suitable selection of high moment stabilization layers, the noise at higher densities, within the percolation density limit, can be substantially reduced. Third harmonic ratio studies indicate that the partial erasure occurs above ~900 kfci. Using a high-resolution high-Q MFM, it is possible to obtain stable and nonpercolating high density patterns up to 1000 kfci on media with tBr = 0.22 memu/[cm.sup.2] and Hc ~ 4500 Oe. This results in practical designs of media for recording densities > 150 Gbits/[in.sup.2]. Index Terms--Magnetic force microscope (MFM), noise power, percolation, synthetic ferrimagnetic media, third harmonic ratio.

Synthetic ferrimagnetic media comprised of two magnetic layers tend to exhibit larger nonlinear transition shift (NLTS) compared to single magnetic layer conventional media. NLTS is reduced by increasing the antiferromagnetic exchange field (Hex) and especially by employing a lower layer with high magnetization and thickness product (Mst). Due to the lower switching field of the stabilization layer, the position of the transition during writing is farther downstream than that of the upper layer. We suggest that, at high densities, the pinning of the lower layer transition below the nearest neighboring upper layer transition leads to a reduction of demagnetizing fields and therefore NLTS. [ABSTRACT FROM AUTHOR]

Brachybacterium sp. strain LB25 produces a maltooligosaccharide-forming amylase that improves product selectivity in water-miscible organic solvents. The enzyme hydrolyzed starch to produce maltotriose primarily. The structural gene encoding the amylase from strain LB25 was cloned and sequenced. The amino acid sequence of the product showed significant similarity (45 to 49%) to amylases from the genus Streptomyces. The amylase gene was expressed in Escherichia coli, but the specific activity of the recombinant amylase was lower than that of the amylase purified from strain LB25.

A bacterium that secretes maltooligosaccharide-forming amylase in a medium containing 12.5% (vol/vol) dimethylsulfoxide (DMSO) was isolated and identified as Brachybacterium sp. strain LB25. The amylase of the strain was purified from the culture supernatant, and its molecular mass was 60 kDa. The enzyme was stable at pH 7.0-8.5 and active at pH 6.0-7.5. The optimum temperature at pH 7.0 was 35 degrees C in the presence of 5 mM CaCl(2). The enzyme hydrolyzed starch to produce maltotriose primarily. The enzyme was active in the presence of various organic solvents. Its yield and product selectivity of maltooligosaccharides in the presence of DMSO or ethanol were compared with those of the industrial maltotriose-forming amylase from Microbacterium imperiale. Both enzymes improved the production selectivity of maltotriose by the addition of DMSO or ethanol. However, the total maltooligosaccharide yield in the presence of the solvents was higher for LB25 amylase than for M. imperiale amylase.