The invention relates to aspartic proteases, and particularly to aspartic proteases for plants. Disclosed are modified plant aspartic proteases, and methods for their manufacture, and uses thereof. Particularly contemplated are the uses of aspartic proteases in clotting milk.

The present invention relates to debriding compositions in the form of an aqueous gel. Particularly, the present invention relates to a debriding composition comprising a proteolytic enzyme mixture obtained from bromelain present in a dry form, and an aqueous gel carrier, wherein, prior to use, the proteolytic enzyme mixture being admixed with the aqueous gel carrier to form a debriding composition useful for debridement and treatment of c wounds.

The present disclosure provides a method of covalently modifying a biological macromolecule, the method comprising subjecting a reaction mixture comprising: (a) a biological macromolecule comprising one or more thiol groups; and (b) a molecule comprising one or more olefin or alkyne moieties to a radical reaction under conditions sufficient to produce the covalently modified biological macromolecule. The present disclosure also provides a method of covalently modifying a biological macromolecule, the method comprising subjecting a reaction mixture comprising: (a) a molecule comprising one or more thiol groups; and (b) a biological macromolecule comprising one or more olefin or alkyne moieties to a radical reaction under conditions sufficient to produce the covalently modified biological macromolecule. The present disclosure further provides a covalently modified biological macromolecule prepared by any of the disclosed methods. The covalently modified biological macromolecules may be further crosslinked to form a scaffold.

The present invention relates to a method of forming a peptide of Formula (I) (P.sup.1-Xaa.sup.1-Xaa.sup.2-P.sup.2) by ligating a first peptide of Formula (II) (P.sup.1-Xaa.sup.1-XR, wherein X is O or S) to a second peptide of Formula (II I) (Xaa.sup.1-Xaa.sup.2-P.sup.2) by enzymatically cleaving the bond between Asx and X in the first peptide of Formula (II) and ligating the fragment P.sup.1-Asx of the first peptide to the second peptide of Formula (III), wherein the enzymatic cleavage and ligation reaction is catalyzed by butelase 1 (SEQ ID NO: 1) and the peptide of Formula (I) is a depsipeptide, preferably a thiodepsipeptide. Further encompassed are peptides and dendrimeric peptide assemblies prepared using the presently disclosed method, as well as use of the dendrimeric peptide assemblies as a vaccine, medicament, or diagnostic agent, particularly as an antimicrobial agent.

The present invention provides an isolated protein exhibiting an antiaggregating activity and/or disaggregating activity toward a target protein comprising an extended polyQ stretch. The protein comprises a Zn.sup.2+-binding region, wherein the conserved motif is HxxEHx.sub.75-80E and x is any amino acid. The nucleic acid construct encoding said protein as well as the corresponding mRNA sequence are also provided. The protein, the nucleic acid construct or mRNA sequence are for use in a method for prevention or treatment of a neurodegenerative disease that is caused by aggregates comprising at least one target protein and/or by the mRNA encoding for said target protein, wherein the target protein causes e.g. Huntington's disease or Machado-Joseph disease.

Certain components of crude bromelain extract have surprisingly been found to not support, or to interfere with, the anti-inflammatory benefit of bromelain. By removing the detrimental components, the remaining component(s) have increased anti-inflammatory effectiveness.

A method of creating a genetically altered plant and parts thereof with a chimeric protein comprising a first domain, a second domain, and a third domain, wherein said first domain comprises either i) a recognition element comprising a Proteinase K sequence, or BPI/LBP sequence, or ii) a lysis element comprising a thionin sequence, said second domain comprises either i) a recognition element comprising a sequence selected from Proteinase K sequence, or BPI/LBP sequence, or ii) a lysis element comprising a thionin sequence wherein the second domain is an element that is different from the element of the first domain and said third domain comprises a linker; wherein said linker separates said first domain from said second domain such that said first domain and said second domain can each fold into its appropriate three-dimensional shape and retains its activity.

Pharmaceutical formulations of orally administered proteins can be stabilized from oxidative degradation and inactivation in the stomach and GI tract by the addition of an antioxidant.

The present disclosure provides a method of covalently modifying a biological macromolecule, the method comprising subjecting a reaction mixture comprising: (a) a biological macromolecule comprising one or more thiol groups; and (b) a molecule comprising one or more olefin or alkyne moieties to a radical reaction under conditions sufficient to produce the covalently modified biological macromolecule. The present disclosure also provides a method of covalently modifying a biological macromolecule, the method comprising subjecting a reaction mixture comprising: (a) a molecule comprising one or more thiol groups; and (b) a biological macromolecule comprising one or more olefin or alkyne moieties to a radical reaction under conditions sufficient to produce the covalently modified biological macromolecule. The present disclosure further provides a covalently modified biological macromolecule prepared by any of the disclosed methods. The covalently modified biological macromolecules may be further crosslinked to form a scaffold.

A process for preparing a milk protein hydrolysate comprising hydrolysing a milk-based proteinaceous material with a microbial alkaline serine protease in combination with bromelain, a protease from Aspergillus and a protease from Bacillus.