Binaural rendering from microphone array signals of arbitrary geometry.

A method of binaural rendering from microphone array signals of arbitrary geometry is proposed. To reproduce binaural signals from microphone array recordings at a remote location, a spherical microphone array is generally used for capturing a soundfield. However, owing to the lack of flexibility in the microphone arrangement, the single spherical array is sometimes impractical for estimating a large region of a soundfield. We propose a method based on harmonic analysis of infinite order, which allows the use of arbitrarily placed microphones. In the synthesis of the estimated soundfield, a spherical-wave-decomposition-based binaural rendering is also formulated to take into consideration the distance in measuring head-related transfer functions. We develop and evaluate a composite microphone array consisting of multiple small arrays. Experimental results including those of listening tests indicate that our proposed method is robust against change in listening position in the recording area.

Properties of mycelial aggregate-specific lectin of Pleurotus cornucopiae produced in Pichia pastoris.

cDNA of a mycelial aggregate-specific lectin of Pleurotus cornucopiae was expressed in Pichia pastoris, and the expression product was purified and characterized. The product was functional, and the hemagglutinating activity was inhibited most strongly by the addition of N-acetyl-D-galactosamine as was the native lectin. The native lectin is a glycoprotein having five glycosylation recognition signals, and the expression product showed slightly larger molecular mass than that of the native one due to further glycosylation.

Molecular properties of mycelial aggregate-specific lectin of Pleurotus cornucopiae.

By cloning and sequencing cDNA, the primary structure of a mycelial aggregate-specific lectin of Pleurotus cornucopiae was determined. The amino acid sequence was novel and elucidated unique properties of this lectin: It was composed of 373 amino acids, 33 of which constitute a signal sequence. The sequence of the mature lectin consisted of two homologous regions having five glycosylation recognition signals and six cysteine residues. However, the distribution of these elements in the two regions was biased. Expression of cDNA in Escherichia coli and Pichia pastoris revealed the requirement of glycosylation to produce the functional lectin. Gel filtration followed by gel electrophoretic analyses of the purified lectin showed that the active component moved faster than the bulk of the protein, suggesting that the most active lectin formed an oligomer of subunits through disulfide bonds. From these observations, a model for the structure of the active form of this lectin is proposed. Southern hybridization using the cDNA as a probe revealed the presence of several genes. The lectin gene was composed of five exons and five introns.

Production of fruiting-body lectins of Pleurotus cornucopiae in methylotrophic yeast Pichia pastoris.

Fruiting-body lectin genes obtained from Pleurotus cornucopiae were expressed in Pichia pastoris Because of glycosylation of the products, their molecular mass was larger than that of the corresponding native lectins. They showed binding activity to porcine stomach mucin in the enzyme-linked lectin assay system, but did not agglutinate red blood cells.

Two genes encoding fruit body lectins of Pleurotus cornucopiae: sequence similarity with the lectin of a nematode-trapping fungus.

Our previous studies on the fruit body lectin of Pleurotus cornucopiae revealed the existence of three isolectins, composed of two homodimers and one heterodimer of 16- and 15-kDa subunits. In this study, two genes encoding the lectins were cloned and characterized. Both genes encoded 144 amino acids and only 5 amino acids were different within the coding region, but the nucleotide sequences of the 5'-upstream and 3'-downstream regions differed extensively. Southern hybridization with gene-specific probes showed that one gene encoded the 16-kDa and the other encoded the 15-kDa subunit. Functional lectins were synthesized in Escherichia coli under the direction of these genes. On SDS-PAGE, the recombinant lectins showed the same banding patterns as the native lectins. In amino acid sequence, these lectins showed extensive similarity with the lectin from a nematode-trapping ascomycete fungus, Arthrobotrys oligospora, suggesting that the lectins might also function in capturing nematodes.