Abstract: The present invention relates to a process for treating an oil comprising a chlorophyll substrate, the process comprising contacting the oil with a polypeptide having decolorase activity or a composition comprising the polypeptide, wherein the polypeptide is selected from the group consisting of: a. a polypeptide which has at least 80% identity to amino acids 1 to 318 of SEQ ID NO: 1; and, b. a polypeptide encoded by a nucleic acid sequence that has at least 80% identity to the nucleic acid sequence of SEQ ID NO: 2.

Abstract: The present invention relates to a process for treating an oil comprising a chlorophyll substrate, the process comprising contacting the oil with a polypeptide having decolorase activity or a composition comprising the polypeptide, wherein the polypeptide is selected from the group consisting of: a. a polypeptide which has at least 80% identity to amino acids 1 to 318 of SEQ ID NO: 1; and, b. a polypeptide encoded by a nucleic acid sequence that has at least 80% identity to the nucleic acid sequence of SEQ ID NO: 2.

Abstract: The present invention relates to a process for treating an oil comprising a chlorophyll substrate, the process comprising contacting the oil with a polypeptide having decolorase activity or a composition comprising the polypeptide, wherein the polypeptide is selected from the group consisting of: a. a polypeptide which has at least 80% identity to amino acids 1 to 318 of SEQ ID NO: 1; and, b. a polypeptide encoded by a nucleic acid sequence that has at least 80% identity to the nucleic acid sequence of SEQ ID NO: 2.

Abstract: The present invention relates to a polypeptide having proline-specific endoprotease activity, selected from the group consisting of i. a polypeptide comprising a mature polypeptide sequence of SEQ ID NO: 2; ii. a polypeptide that has least 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identity to the mature polypeptide sequence of SEQ ID NO: 2; iii. a polypeptide encoded by a nucleic acid that hybridizes under medium stringency, preferably under high stringency conditions to the complementary strand of the mature polypeptide coding sequence of SEQ ID NO:1; iv. a polypeptide encoded by a nucleic acid that has at least 70%, 75% 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the mature polypeptide coding sequence of SEQ ID NO: 1. The invention further relates to a method of producing the polypeptide and a process for the preparation of a food or feed product wherein the polypeptide is used.

Abstract: The present invention relates to an alpha amylase enzyme and to its use in the food, feed and non-food industry.

Abstract: The present invention relates to a polypeptide having proline-specific endoprotease activity, wherein the polypeptide has less than 70% residual activity when the polypeptide has been kept at a temperature of 65° C. for 15 min. The invention further relates to a polypeptide having proline-specific endoprotease activity comprising an amino acid sequence according to SEQ ID NO: 1, wherein SEQ ID NO: 1 comprises at least one amino acid substitution selected from the group consisting of P469A, P469C, P469D, P469E, P469F, P469G, P469H, P469I, P469K, P469L, P469M, P469N, P469Q, P469R, P469S, P469T, P469V, P469W, P469Y, a nucleic acid encoding a polypeptide having proline-specific endoprotease activity, a method of making a variant polypeptide having proline-specific endoprotease activity, a recombinant host cell and a method of producing the polypeptide and a process for the preparation of a food or feed product wherein the polypeptide is used.

Abstract: The invention relates to a method for enzymatically synthesizing an (oligo)peptide, comprising coupling (a) an (oligo)peptide C-terminal ester or thioester and (b) an (oligo)peptide nucleophile having an N-terminally unprotected amine, wherein the coupling is carried out in a fluid comprising water, and wherein the coupling is catalyzed by a subtilisin BPN? variant or a homolog thereof, which comprises the following mutations compared to subtilisin BPN? represented by SEQUENCE ID NO: 2 or a homolog sequence thereof: a deletion of the amino acids corresponding to positions 75-83; a mutation at the amino acid position corresponding to S221, the mutation being S221C or S221 selenocysteine; preferably a mutation at the amino acid position corresponding to P225 wherein the amino acid positions are defined according to the sequence of subtilisin BPN? represented by SEQUENCE ID NO: 2. Further, the invention relates to an enzyme suitable for use as a catalyst in a method of the invention.

Abstract: The present invention relates to a polypeptide having proline-specific endoprotease activity, wherein the polypeptide has less than 70% residual activity when the polypeptide has been kept at a temperature of 65° C. for 15 min.

Abstract: The invention relates to a method for enzymatically synthesizing an (oligo)peptide, comprising coupling (a) an (oligo)peptide C-terminal ester or thioester and (b) an (oligo)peptide nucleophile having an N-terminally unprotected amine, wherein the coupling is carried out in a fluid comprising water, and wherein the coupling is catalyzed by a subtilisin BPN? variant or a homologue thereof, which comprises the following mutations compared to subtilisin BPN? represented by SEQUENCE ID NO: 2 or a homologue sequence thereof : a deletion of the amino acids corresponding to positions 75-83; a mutation at the amino acid position corresponding to S221, the mutation being S221C or S221 selenocysteine; preferably a mutation at the amino acid position corresponding to P225 wherein the amino acid positions are defined according to the sequence of subtilisin BPN? represented by SEQUENCE ID NO: 2. Further, the invention relates to an enzyme suitable for use as a catalyst in a method of the invention.

Abstract: The invention relates to a method for enzymatically synthesizing an (oligo)peptide, comprising coupling (a) an (oligo)peptide C-terminal ester or thioester and (b) an (oligo)peptide nucleophile having an N-terminally unprotected amine, wherein the coupling is carried out in a fluid comprising water, and wherein the coupling is catalyzed by a subtilisin BPN? variant or a homo-log thereof, which comprises the following mutations compared to subtilisin BPN? represented by SEQUENCE ID NO: 2 or a homolog sequence thereof: a deletion of the amino acids corresponding to positions 75-83; a mutation at the amino acid position corresponding to S221, the mutation being S221C or S221 selenocysteine; preferably a mutation at the amino acid position corresponding to P225 wherein the amino acid positions are defined according to the sequence of subtilisin BPN? represented by SEQUENCE ID NO: 2. Further, the invention relates to an enzyme suitable for use as a catalyst in a method of the invention.

Abstract: The present invention relates to a polypeptide having asparaginase activity selected from the group consisting of: (i) a polypeptide having an amino acid sequence comprising the mature polypeptide sequence of SEQ ID NO: 1; (ii) a polypeptide comprising an amino acid sequence that has at least 50% sequence identity with the mature polypeptide sequence of SEQ ID NO: 1; (iii) a polypeptide encoded by a nucleic acid comprising a sequence that hybridizes under medium stringency conditions to the complementary strand of the mature polypeptide encoding sequence of SEQ ID NO: 2; and (iv) a polypeptide comprising an amino acid sequence encoded by a nucleic acid that has at least 50% sequence identity to the mature polypeptide coding sequence of SEQ ID NO: 2. The polypeptide may be used in the preparation of a food product.

Abstract: The present invention relates to a polypeptide having proline-specific endoprotease activity, wherein the polypeptide has less than 70% residual activity when the polypeptide has been kept at a temperature of 65° C. for 15 min.

Abstract: The invention relates to a method for enzymatically synthesizing an (oligo)peptide, comprising coupling (a) an (oligo)peptide C-terminal ester or thioester and (b) an (oligo)peptide nucleophile having an N-terminally unprotected amine, wherein the coupling is carried out in a fluid comprising water, and wherein the coupling is catalyzed by a subtilisin BPN? variant or a homologue thereof, which comprises the following mutations compared to subtilisin BPN? represented by SEQUENCE ID NO: 2 or a homologue sequence thereof: a deletion of the amino acids corresponding to positions 75-83; a mutation at the amino acid position corresponding to S221, the mutation being S221C or S221 selenocysteine; preferably a mutation at the amino acid position corresponding to P225 wherein the amino acid positions are defined according to the sequence of subtilisin BPN? represented by SEQUENCE ID NO: 2. Further, the invention relates to an enzyme suitable for use as a catalyst in a method of the invention.

Abstract: The present invention relates to an alpha amylase enzyme and to its use in the food, feed and non-food industry.

Abstract: The present invention relates to a polypeptide having proline-specific endoprotease activity, wherein the polypeptide has less than 70% residual activity when the polypeptide has been kept at a temperature of 65° C. for 15 min. The invention further relates to a polypeptide having proline-specific endoprotease activity comprising an amino acid sequence according to SEQ ID NO: 1, wherein SEQ ID NO: 1 comprises at least one amino acid substitution selected from the group consisting of P469A, P469C, P469D, P469E, P469F, P469G, P469H, P469I, P469K, P469L, P469M, P469N, P469Q, P469R, P469S, P469T, P469V, P469W, P469Y, a nucleic acid encoding a polypeptide having proline-specific endoprotease activity, a method of making a variant polypeptide having proline-specific endoprotease activity, a recombinant host cell and a method of producing the polypeptide and a process for the preparation of a food or feed product wherein the polypeptide is used.

Abstract: The present invention relates to a polypeptide having proline-specific endoprotease activity, selected from the group consisting of i. a polypeptide comprising a mature polypeptide sequence of SEQ ID NO: 2; ii. a polypeptide that has least 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identity to the mature polypeptide sequence of SEQ ID NO: 2; iii. a polypeptide encoded by a nucleic acid that hybridizes under medium stringency, preferably under high stringency conditions to the complementary strand of the mature polypeptide coding sequence of SEQ ID NO:1; iv. a polypeptide encoded by a nucleic acid that has at least 70%, 75% 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identity to the mature polypeptide coding sequence of SEQ ID NO: 1. The invention further relates to a method of producing the polypeptide and a process for the preparation of a food or feed product wherein the polypeptide is used.

Abstract: The present invention relates to novel lipase polynucleotide sequences, their corresponding proteins as well as ways of manufacturing said sequences and said proteins and use of the proteins in the preparation of food compositions. The invention further relates to methods for releasing proteins from the exterior of a host cell as well as to a method for killing micro-organisms.

Abstract: The present invention relates to a method for improving protein yield. The method comprises modifying the value of a set of relevant protein features to fall within an optimal range or to become more close to an optimal value for one or more protein features in the eukaryotic host.

Abstract: The present invention relates to newly identified asparaginase polypeptide variants of SEQ ID NO: 3 and to polynucleotide sequences that encode such novel asparaginase variants. Furthermore the invention relates to the use of these novel asparaginase variants in industrial processes.

Abstract: The present invention relates to a method for producing a cyclic peptide compound or a salt thereof which comprises contacting a cyclic lipopeptide compound or a salt thereof with an acylase derived from a microorganism belonging to the genus Pseudomonas to deacylate the lipid acyl moiety of said cyclic lipopeptide.