Abstract: This invention relates to an inexpensive phytase with a low Km value for phytic acid, DNA coding for the phytase, recombinant DNA having the DNA introduced thereinto, a transformant carrying the recombinant DNA, a process for preparing a phytase by use of the transformant, and an animal feed comprising the phytase.

Abstract: Provided is an isolated phytase derived from a microorganism. The microorganism is preferably from the genus Monascus. The phytase has a Michaelis constant of 10 to 110 &mgr;M when phytic acid is used as a substrate. A process for producing the phytase is also provided as is an animal feed comprising the phytase. The phytase is preferably isolated from Monascus anka IFO 30873. The phytase has a Km of 107 &mgr;m when phytic acid is used as a substrate, the optimum pH is 2.5, the optimum temperature is 45° C., the molecular weight of the phytase is 140 kDa when measured by gel filtration, and the isolectric point is 5.2 using chromatofocusing.

Abstract: The present invention provides phytases having low Km values for phytic acid, a process for producing the phytases by using a microorganism having the ability to produce and accumulate the phytases and feed containing the phytases.

Abstract: The present invention relates to a polypeptide having 25-hydroxyvitamin D3-1&agr;-hydroxylase activity, being useful for the prevention, diagnosis and therapeutic treatment of adult diseases such as osteoporosis induced by the decrease of active type vitamin D3 and catalyzing the final stage of vitamin D3 activation; and the gene encoding the polypeptide.

Abstract: The phytase is preferably isolated from Monascus anka IFO 30873. The phytase has a Km of 20 &mgr;m when phytic acid is used as a substrate, the optimum pH is 6.0, the optimum temperature is 50° C., the molecular weight of the phytase is 120 kDa when measured by gel filtration, and the isolectric point is 4.8 using chromatofocusing.

Abstract: This invention relates to an inexpensive phytase with a low Km value for phytic acid, DNA coding for the phytase, recombinant DNA having the DNA introduced thereinto, a transformant carrying the recombinant DNA, a process for preparing a phytase by use of the transformant, and an animal feed comprising the phytase.

Abstract: The present invention relates to a polypeptide having 25-hydroxyvitamin D3-1&agr;-hydroxylase activity, being useful for the prevention, diagnosis and therapeutic treatment of adult diseases such as osteoporosis induced by the decrease of active type vitamin D3 and catalyzing the final stage of vitamin D3 activation; and the gene encoding the polypeptide. In accordance with the present invention, the following can be provided; a polypeptide having 25-hydroxyvitamin D3-1&agr;-hydroxylase activity, DNA encoding the polypeptide, a recombinant DNA prepared by inserting the DNA in a vector, a transformant carrying the recombinant DNA, a method for preparing 25-hydroxyvitamin D3-1&agr;-hydroxylase by using the transformant, a method for preparing 1&agr;, 25-dihydroxyvitamin D3 comprising using the polypeptide having 25-hydroxyvitamin D3-1&agr;-hydroxylase activity, and an antibody recognizing the polypeptide.

Abstract: Provided is an isolated phytase derived from a microorganism. The microorganism is preferably from the genus Monascus. The phytase has a Michaelis constant of 10 to 110 &mgr;M when phytic acid is used as a substrate. A process for producing the phytase also is provided, as is an animal feed comprising the phytase.

Abstract: This invention relates to an inexpensive phytase with a low Km value for phytic acid, DNA coding for the phytase, recombinant DNA having the DNA introduced thereinto, a transformant carrying the recombinant DNA, a process for preparing a phytase by use of the transformant, and an animal feed comprising the phytase.

Abstract: The present invention provides monoclonal antibodies and humanized antibodies which react specifically with a human interleukin-5 receptor .alpha. chain. The invention also provides hybridomas and transformants which produce the antibodies, the monoclonal antibodies and humanized antibodies, a method for detecting an interleukin-5 receptor .alpha. chain immunologically by means of these antibodies, as well as a method for diagnosing and treating diseases such as chronic bronchial asthma by means of the monoclonal antibodies and humanized antibodies. The present invention is useful for diagnosis or treatment of diseases such as chronic bronchial asthma.

Abstract: The invention relates to a process for producing a desired substance by culturing a transformant in a medium until the desired substance is accumulated in the culture and then recovering the desired substance, the transformant being obtained by transforming an acetic acid-resistant microorganism of the genus Escherichia with a recombinant plasmid carrying a gene involved in production of the desired substance. The present process enables cells to be cultured easily at high density while the desired substance can be efficiently produced.

Abstract: Disclosed is a process for producing amino acids such as L-threohine and L-lysine, which comprises culturing, in a medium containing methanol as a major carbon source, a microorganism which belongs to the genus Methylobacillus and which has an ability to produce the amino acid(s) and resistance to at least one member selected from the group consisting of L-threonine, L-lysine and an amino acid analogue, said microorganism being obtained by mutation of a parent strain which belongs to the genus Methylobacillus and which has an enhanced sensitivity to at least one of an antibiotic and an amino acid analogue; allowing the amino acid(s) to accumulate in the culture; and recovering the amino acid(s) therefrom.

Abstract: L-phenylalanine is produced by using a microorganism belonging to the species Citrobacter freundii, Erwinia herbicola, Enterobacter cloacae, Klebsiella oxytoca, Salmonella typhimurium, Bacillus cereus, Flavobacterium suaveolens, Serratia marcescens, Pseudomonas putida, Enterobacter cloacae, Proteus mirabilis, Paracoccus denitrificans, Arthrobacter globiformis, Bacillus sphaericus, Corynebacterium hydrocarboclastus, Kluyvera micum or Microbacterium ammoniaphilum and having the ability to convert phenylpyruvic acid into L-phenylalanine in the presence of an amino group donor; or fumaric acid and ammonium ion or urea.