Danisco A/s

Dupont Nutrition Biosciences Aps

Syngenta Participations Ag

Janne Brunstedt

Jørn Borch Søe

Jørn Dalgaard Mikkelsen

Charlotte Horsmans Poulsen

Rene Mikkelsen

Henrik Pedersen

Richard Ray Bott

Marguerite A Cervin

Susan Mampusti Madrid

Masoud Rajabi Zargahi

Jorn Borch Soe

Charlotte Refdahl Thoudahl

Morten Krog Larsen

Steen Guldager Petersen

Jens Frisbaek Sorensen

Jorn Dalgaard Mikkelsen

Klaus Kristian Nielsen

Lone Broend Miller

Tove Martel Ida Else Christensen

Anette Amstrup Pedersen

Morten Jorsboe

Kirsten Jorgensen

Rikke H Lorentzen

Anne Kroll Kristensen

Jens Frisbaæk Sørensen

Tina Jørgensen

Tina Lillan Jorgensen

Lene Lauridsen

Morten J&thgr;rsboe

Jens Frisbæk Sorensen

Charlotte Johansen Vedel

Rikke Hoegh Lorentsen

Birgitte Ø Wittschieben

Lene B Jensen

Tina Lillan Jørgensen

Jens Frisbæk SØRENSEN

Smith Anja Hemmingsen Kellett

The present invention provides methods and uses for treating pyropheophytin-containing compositions, particularly in order to remove pyropheophytin therefrom. The compositions are typically plant, algal, or bacterial derived products such as vegetable oils. The method comprises a step of contacting the compositions with an enzyme having pyropheophytinase activity. Also provided are related apparatus and products for performing such methods and uses.

Method for treating pyropheophytin-containing compositions

In one aspect, there is provided a process for treating a plant oil, comprising a step of contacting the oil with an enzyme, wherein the enzyme is capable of hydrolyzing an a' or b&#x2032; stereoisomer of chlorophyll or a chlorophyll derivative.

Process modifications to enhance chlorophyll degradation

The present invention provides a method for preparing a variant lipid acyltransferase enzyme by expressing a nucleotide sequence encoding a lipid acyltransferase which may comprise at least one modification at a position(s) which corresponds in the encoded amino acid sequence to an amino acid(s) located in a) the canyon region of the enzyme (i.e. preferably amino acid residues 31, 27, 85, 86, 119, and 120); and/or b) insertion site 1 (i.e. amino acid residues 22-36) and/or c) insertion site 2 (i.e. amino acid residues 74-88), wherein the canyon region, insertion site 1 and/or insertion site 2 are defined as that region which when aligned based on primary or tertiary structure corresponds to the canyon region, insertion site 1 or insertion site 2 (or the corresponding amino acid residues taught above) of the enzyme shown herein as SEQ ID No. 16 or 6 in a host organism.

Lipid acyltransferase proteins and methods of making them

A fungal wild-type lipolytic enzyme having a higher ratio of activity on polar lipids compared with triglycerides, wherein the enzyme preferably has a phospholipid:triglyceride activity ratio of at least 4. Preferably, the lipolytic enzyme according to the present invention has a glycolipid:triglyceride hydrolyzing activity ratio of at least 1.5. In one embodiment, the fungal lipolytic enzyme according to the present invention comprises an amino acid sequence as shown in SEQ ID NO: 1 or SEQ ID No. 2 or SEQ ID No. 4 or SEQ ID No. 6 or an amino acid sequence which has at least 90% identity thereto. The present invention further encompasses a nucleic acid encoding a fungal lipolytic enzyme, which nucleic acid is selected from the group consisting of: (a) a nucleic acid comprising a nucleotide shown in SEQ ID No. 3, SEQ ID No. 5 or SEQ ID No. 7; (b) a nucleic acid which is related to the nucleotide sequence of SEQ ID No. 3, SEQ ID No. 5 or SEQ ID No. 7 by the degeneration of the genetic code; and (c) nucleic acid comprising a nucleotide sequence which has at least 90% identity with the nucleotide sequence shown in SEQ ID No. 3, SEQ ID No. 5 or SEQ ID No. 7.

Fungal lypolytic and amylase enzyme composition and methods using the same

Fungal lipolytic enzymes, nucleic acids encoding, and uses thereof

A selection method for selecting from a population of cells one or more selectable genetically transformed cells is described. The population of cells comprises selectable genetically transformed cells and possible non-transformed cells. Each of the selectable genetically transformed cells comprises a first expressable nucleotide sequence encoding a first expression product; and optionally a second expressable nucleotide sequence encoding a second expression product and/or a third expressable nucleotide sequence encoding a third expression product. A component is utilisable by the selectable genetically transformed cells by action of the first expressable nucleotide sequence or the first expression product and optionally by action of the optional second expressable nucleotide sequence or the optional second expression product and/or by, action of the optional third expressable nucleotide sequence or the optional Third expression product. The component can be present in an amount that is toxic to the non-transformed cells.

Selection method

A process for treating a pectin with a pectin methyl esterase (PME) is descibed. Here, the PME is not a plant PME&mdash;but the PME is capable of exhibiting at least one plant PME property; wherein the at least one plant PME property comprises at least block&mdash;wise de-esterification of the pectin.

Process for enzymatically modifying pectin

A UDP-galactose epimerase enzyme is described. In addition, there is described a nucleotide sequence coding for the same.

Cloning of UDP-galactose epimerase

Isolated proteins having anti-fungal activity against at least Cercospora spp. The proteins contain an amino acid sequence which has at least 95% sequence identity to any of the following sequences: SEQ ID NO:3 wherein the amino acid in position 80 is alanine instead of valine, SEQ ID NO:5 and SEQ ID NO:6. Recombinant DNA molecules encoding such proteins. A vector comprising such DNA which is expressible in plants and which is linked to a plant operable promoter and terminator. Plants transformed with such recombinant DNA; the progeny of such plants which contain the DNA stably incorporated and hereditable in a Mendelian manner, and/or the seeds of such plants or such progeny.

Antimicrobial proteins

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Roskilde, Denmark

Janne Brunstedt