Abstract: The present invention relates to the production process of biotin by fermentation using genetically engineered microorganisms, including Escherichia coli and Pseudomonas mutabilis, and DNA sequences and vectors to be used in such process.

Abstract: The present invention relates generally to modified Bacillus thuringiensis (Bt) insecticidal crystal proteins, also referred to as mutant toxins, with enhanced toxicity against a variety of insect genera, particularly mosquitos. The invention provides modified Bt Cry4Ba proteins, or mutant toxins, which have toxicity-enhancing sequence modifications at one or more positions within the amino acid sequence of the protein. The invention also provides polynucleotides encoding modified Cry4Ba proteins. The invention also provides insecticidal compositions comprising mutant toxins with a new or broadened insecticidal spectrum, and insecticidal compositions comprising polynucleotides encoding the modified Cry4Ba proteins.

Abstract: A process for the preparation of L-amino acids, in particular L-threonine is disclosed herein. In particular, a process for the preparation of L-amino acids in Enterobacteriaceae, comprising fermenting, in a medium, Enterobacteriaceae which produce L-amino acid and in which E. coli ahpC and ahpF is overexpressed, and concentrating the L-amino acids in the medium or in the Enterobacteriaceae is disclosed.

Abstract: The present application relates to methods for growing crystals of both the uncomplexed and complexed forms of ?-secretase (BACE) polypeptide. Polypeptides used herein are derived from human BACE which is also known by the synonyms “mamapsin 2”, “human ?-site APP-cleaving enzyme, and Asp2”. The present application also relates to crystalline forms of uncomplexed BACE and the three-dimensional structure of BACE, as determined from the crystals. In addition, the present application relates to the use of crystalline forms of BACE to identify ligands, preferably inhibitors (antagonists), which bind to, and preferably inhibit the enzymatic activity of, BACE. Furthermore, the present application relates to nucleic acid sequences encoding BACE polypeptide, and methods for making BACE in greater quantity than prior methods, resulting in more effective crystallization.