Secreted proteases from pathogenic fungi.

https://zenodo.org/record/1259499/files/article.pdf

Food-processing enzymes from recombinant microorganisms—a review

Flavourzyme is sold as a peptidase preparation from Aspergillus oryzae. The enzyme preparation is widely and diversely used for protein hydrolysis in industrial and research applications. However, detailed information about the composition of this mixture is still missing due to the complexity. The present study identified eight key enzymes by mass spectrometry and partially by activity staining on native polyacrylamide gels or gel zymography. The eight enzymes identified were two aminopeptidases, two dipeptidyl peptidases, three endopeptidases, and one α-amylase from the A. oryzae strain ATCC 42149/RIB 40 (yellow koji mold). Various specific marker substrates for these Flavourzyme enzymes were ascertained. An automated, time-saving nine-step protocol for the purification of all eight enzymes within 7 h was designed. Finally, the purified Flavourzyme enzymes were biochemically characterized with regard to pH and temperature profiles and molecular sizes.

Flavourzyme, an Enzyme Preparation with Industrial Relevance: Automated Nine-Step Purification and Partial Characterization of Eight Enzymes

Biological potential of protein hydrolysates and peptides from common bean (Phaseolus vulgaris L.): A review

Molecular biology of the Koji molds.

A novel serine carboxypeptidase (EC 3.4.16.1) was found in an Aspergillus oryzae fermentation broth and was purified to homogeneity. This enzyme has a molecular weight of ca. 67,000, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its specific activity is 21 U/mg for carbobenzoxy (Z)-Ala-Glu at pH 4.5 and 25 degrees C. It has a ratio of bimolecular constants for Z-Ala-Lys and Z-Ala-Phe of 3.75. Optimal enzyme activity occurs at pH 4 to 4.5 and 58 to 60 degrees C for Z-Ala-Ile. The N terminus of this carboxypeptidase is blocked. Internal fragments, obtained by cyanogen bromide digestion, were sequenced. PCR primers were then made based on the peptide sequence information, and the full-length gene sequence was obtained. An expression vector that contained the recombinant carboxypeptidase gene was used to transform a Fusarium venenatum host strain. The transformed strain of F. venenatum expressed an active recombinant carboxypeptidase. In F. venenatum, the recombinant carboxypeptidase produced two bands which had molecular weights greater than the molecular weight of the native carboxypeptidase from A. oryzae. Although the molecular weights of the native and recombinant enzymes differ, these enzymes have very similar kinetic parameters.

Purification, Characterization, and Heterologous Expression in Fusarium venenatum of a Novel Serine Carboxypeptidase from Aspergillus oryzae

A non-specific aminopeptidase from Aspergillus.

The present invention relates to a method for producing a protein composition soluble in organic solvents, comprising mixing a protein of interest with a surfactant and a water immiscible organic solvent in amounts and under conditions conducive to the formation of a reverse micelle solution, and evaporating the resulting reverse micelle solution to dryness.

Method for solubilizing proteins in organic solvents

The present invention relates to isolated polypeptides having aminopeptidase activity and isolated nucleic acid sequences encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the nucleic acid sequences as well as methods for producing and using the polypeptides.

Polynucleotides encoding polypeptides having aminopeptidase activity

La presente invention porte sur des polypeptides isoles ayant l'activite d'alpha-glucosidase et sur des polynucleotides isoles codant les polypeptides. L'invention porte egalement sur des produits de recombinaison des acides nucleiques, sur des vecteurs et sur des cellules hotes comprenant les polynucleotides, ainsi que sur des procedes de production et d'utilisation des polypeptides.

Polypeptides ayant l'activite d'alpha-glucosidase et polynucleotides les codant

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