Recombinantly produced hydrophobins from fungal analogues as highly surface-active performance proteins.

Hydrophobins are available from natural resources only in milligram amounts. BASF succeeded in a recombinant production process, up-scaled to pilot plant production in kilogram scale. Strain and protein optimization by modulation of gene expression and generation of fusion proteins finally leads to two class I hydrophobins called H*Protein A and H*Protein B.

Use of laccase as a novel, versatile reporter system in filamentous fungi.

Laccases are copper-containing enzymes which oxidize phenolic substrates and transfer the electrons to oxygen. Many filamentous fungi contain several laccase-encoding genes, but their biological roles are mostly not well understood. The main interest in laccases in biotechnology is their potential to be used to detoxify phenolic substances.

Analysis of mating-dependent transcription of Blakeslea trispora carotenoid biosynthesis genes carB and carRA by quantitative real-time PCR.

The zygomycete fungus Blakeslea trispora is used commercially as natural source of beta-carotene. beta-Carotene production is strongly induced during mating of two strains of the opposite sex and results in the production of the pheromone trisporic acid, which in turn stimulates enhanced beta-carotene biosynthesis. beta-Carotene production is due to the enzymatic activity of phytoene synthase, lycopene cyclase and phytoene dehydrogenase.

A genome-wide transcription analysis of a fungal riboflavin overproducer.

The production of many fine chemicals such as vitamins and amino acids is carried out in bioreactors using microorganisms. Usually, these strains are developed from wild-type organisms by classical mutation and selection. After several generations of strain improvement, no further enhancement can be achieved.

L-amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma. Comparative sequence analysis and characterization of active and inactive forms of the enzyme.

Here we report the cDNA-deduced amino-acid sequence of L-amino-acid oxidase (LAAO) from the Malayan pit viper Calloselasma rhodostoma, which shows 83% identity to LAAOs from the Eastern and Western diamondback rattlesnake (Crotalus adamanteus and Crotalus atrox, respectively). Phylogenetic comparison of the FAD-dependent ophidian LAAOs to FAD-dependent oxidases such as monoamine oxidases, D-amino-acid oxidases and tryptophan 2-monooxygenases reveals only distant relationships. Nevertheless, all LAAOs share a highly conserved dinucleotide-binding fold with monoamine oxidases, tryptophan 2-monooxygenases and various other proteins that also may have a requirement for FAD.

The ornithodorin-thrombin crystal structure, a key to the TAP enigma?

Ornithodorin, isolated from the blood sucking soft tick Ornithodoros moubata, is a potent (Ki = 10(-12) M) and highly selective thrombin inhibitor. Internal sequence homology indicates a two domain protein. Each domain resembles the Kunitz inhibitor basic pancreatic trypsin inhibitor (BPTI) and also the tick anticoagulant peptide (TAP) isolated from the same organism.

Non-repetitive AT-rich sequences are found in intergenic regions of Methanococcus voltae DNA.

AT-rich DNA, which constitutes a distinct fraction of the cellular DNA of the archaebacterium Methanococcus voltae, was shown to consist of non-repetitive sequences dispersed on the chromosome and to lack continuous open reading frames in five out of six randomly analyzed cases. Upon subsequent analysis of intergenic regions, AT-rich sequences were again detected. Transcription start points were mapped in front of three open reading frames.