Abstract: We disclose a food additive comprising a PS4 variant polypeptide, in which the PS4 variant polypeptide is derivable from a parent polypeptide having non-maltogenic exoamylase activity, in which the PS4 variant polypeptide comprises substitutions at the following positions: 6121D, 134, 141, 157, 223, 307 and 334 with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1.

Abstract: The invention provides for a PS4 variant polypeptide derivable from a parent polypeptide having amylase activity which may be selected from the group consisting of: (a) a polypeptide comprising an amino acid mutation at each of positions 33, 34, 121, 134, 141, 146, 157, 161, 178, 179, 223, 229, 272, 303, 307, 309 and 334; (b) a polypeptide comprising an amino acid mutation at each of positions 33, 34, 121, 134, 141, 145, 146, 157, 178, 179, 223, 229, 272, 303, 307 and 334; (c) a polypeptide comprising an amino acid mutation at each of positions 33, 34, 121, 134, 141, 146, 157, 178, 179, 223, 229, 272, 303, 307, 309 and 334; and (d) a polypeptide comprising an amino acid mutation at each of positions 3, 33, 34, 70, 121, 134, 141, 146, 157, 178, 179, 223, 229, 272, 303, 307, 309 and 334; with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1, uses of such a polypeptide as a food or feed additive, and nucleic acids encoding such.

Abstract: We disclose a PS4 variant polypeptide derivable from a parent polypeptide, the parent polypeptide having non-maltogenic exoamylase activity, which PS4 variant polypeptide comprises one or more of the following substitutions: G69P, A141P, G223A, A268P, G313P, S399P and G400P, with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1. Such PS4 variant polypeptides may be used as exo-amylases, particularly as non-maltogenic exoamylases. Combinations of such PS4 variant polypeptides together with Novamyl are disclosed.

Abstract: This is invention relates to amylase polypeptides, and nucleic acids encoding the polpypeptides and uses thereof. The amylases of the present invention have been engineered to have more beneficial qualities. Specifically, the amylases of the current invention show an altered thermostability.

Abstract: This invention relates to amylase polypeptides, and nucleic acids encoding the polpypeptides and uses thereof. The amylases of the present invention have been engineered to have more beneficial qualities. Specifically, the amylases of the current invention show an altered exospecifity.

Abstract: An enzyme is described which enzyme is derived from family 13 of ?-amylases. The enzyme variant is obtainable by modifying a CGTase or a maltogenic ?-amylase. The enzyme is useful in preparing a food or a food product such as bakery products.

Abstract: We describe a food additive comprising a PS4 variant polypeptide, in which the PS4 variant polypeptide is derivable from a parent polypeptide having non-maltogenic exoamylase activity, in which the PS4 variant polypeptide comprises an amino acid mutation at one or more positions selected from the group consisting of: 146, 157, 158, 198, 229, 303, 306, 309, 316 and 353, with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1. Preferably, the PS4 variant polypeptide comprises an amino acid mutation selected from the group consisting of: 146G, 146M, 157M, 158T, 158A, 158S, 198W, 198F, 229P, 303E, 303D, 306T, 306G, 309P, 316S, 316P, 316K, 316Q and 353T, preferably 146G, 157M, 158T, 198W, 229P, 303E, 303D, 306T, 306G, 309P, 316S, 316P or 353T. in highly preferred embodiments, the PS4 variant polypeptide has a sequence selected from SEQ ID NO: 15 to 28.

Abstract: We describe a food additive comprising a PS4 variant polypeptide, in which the PS4 variant polypeptide is derivable from a parent polypeptide having non-maltogenic exoamylase activity, in which the PS4 variant polypeptide comprises an amino acid substitution at position 161 with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1. The PS4 variant polypeptide may further comprise one or more further mutations at a position selected from the group consisting of: 121 and 223, preferably 121F, 121Y, 121W, 223E and 223K, more preferably G121F, G121Y, G121W, G223E and/or G223K, or the group consisting of: 134, 141, 157, 223, 307, 334, 33 and 34, preferably G134R, A141P, I157L, G223A, H307L, S334P, N33Y and D34N. In preferred embodiments, the PS4 variant polypeptide further comprises a mutation at position 87, preferably G87S, a mutation at position 178, preferably L178F, and/or a mutation at position 179, preferably A179T.

Abstract: We describe a food additive comprising a PS4 variant polypeptide, in which the PS4 variant polypeptide is derivable from a parent polypeptide having non-maltogenic exoamylase activity, in which the PS4 variant polypeptide comprises an amino acid substitution at position 121 with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1. The PS4 variant polypeptide may further comprise one or more further mutations at a position selected from the group consisting of: 161 and 223, preferably 161A, 223E and 223K, more preferably S161A, G223E and/or G223K, or the group consisting of: 134, 141, 157, 223, 307, 334, 33 and 34, preferably G134R, A141P, I157L, G223A, H307L, S334P, N33Y and D34N. In preferred embodiments, the PS4 variant polypeptide further comprises a mutation at position 87, preferably G87S, a mutation at position 178, preferably L178F, and/or a mutation at position 179, preferably A179T.

Abstract: We describe a food additive comprising a PS4 variant polypeptide, in which the PS4 variant polypeptide is derivable from a parent polypeptide having non-maltogenic exoamylase activity, in which the PS4 variant polypeptide comprises an amino acid substitution at position 223 with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1. The PS4 variant polypeptide may further comprise one or more further mutations at a position selected from the group consisting of: 121 and 161, preferably 121F, 121Y, 121W and 161A, more preferably G121F, G121Y, G121W and/or S161A, or the group consisting of: 134, 141, 157, 223, 307, 334, 33 and 34, preferably G134R, A141P, I157L, G223A, H307L, S334P, N33Y and D34N. In preferred embodiments, the PS4 variant polypeptide further comprises a mutation at position 87, preferably G87S, a mutation at position 178, preferably L178F, and/or a mutation at position 179, preferably A179T.

Abstract: This invention relates to amylase polypeptides, and nucleic acids encoding the polpypeptides and uses thereof. The amylases of the present invention have been engineered to have more beneficial qualities. Specifically, the amylases of the current invention show an altered exospecifity.

Abstract: This invention relates to amylase polypeptides, and nucleic acids encoding the polpypeptides and uses thereof. The amylases of the present invention have been engineered to have more beneficial qualities. Specifically, the amylases of the current invention show an altered thermostability.

Abstract: We disclose a food additive comprising a PS4 variant polypeptide, in which the PS4 variant polypeptide is derivable from a parent polypeptide having non-maltogenic exoamylase activity, in which the PS4 variant polypeptide comprises substitutions at the following positions: G121D, 134, 141, 157, 223, 307 and 334 with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1.

Abstract: The present invention relates to a component comprising an enzyme for use in a feed comprising strach: wherein the enzyme has amylase activity and is capable of degrading resistant starch.

Abstract: We disclose a PS4 variant polypeptide derivable from a parent polypeptide, the parent polypeptide having non-maltogenic exoamylase activity, which PS4 variant polypeptide comprises one or more of the following substitutions: G69P, A141P, G223A, A268P, G313P, S399P and G400P, with reference to the position numbering of a Pseudomonas saccharophilia exoamylase sequence shown as SEQ ID NO: 1. Such PS4 variant polypeptides may be used as exo-amylases, particularly as non-maltogenic exoamylases. Combinations of such PS4 variant polypeptides together with Novamyl are disclosed.

Abstract: A method of preparing the sugar 1,5-D-anhydrofructose is described. The method comprises treating an &agr;-1,4-glucan with an &agr;-1,4-glucan lyase wherein the enzyme is used in substantially pure form. In a preferred embodiment, if the glucan contains links other than and in addition to the &agr;-1,4-links, the &agr;-1,4-glucan lyase is used in conjunction with a suitable reagent that can break the other links.

Abstract: A method of preparing the sugar 1,5-D-anhydrofructose is described. The method comprises treating an &agr;-1,4-glucan with an &agr;-1,4-glucan lyase wherein the enzyme is used in substantially pure form. In a preferred embodiment, if the glucan contains links other than and in addition to the &agr;-1,4-links, the &agr;-1,4-glucan lyase is used in conjunction with a suitable reagent that can break the other links.

Abstract: A method of preparing the sugar 1,5-D-anhydrofructose is described. The method comprises treating an alpha -1,4-glucan with an alpha -1,4-glucan lyase wherein the enzyme is used in substantially pure form. In a preferred embodiment, if the glucan contains links other than and in addition to the alpha -1,4-links, the alpha -1,4-glucan lyase is used in conjunction with a suitable reagent that can break the other links.

Abstract: A method of preparing .alpha.-1,4-glucan lyase enzymes is described. The method comprises isolating the enzymes from a fungally infected algae. The amino acid sequences of the enzymes have been determined. The nucleic acid sequences coding for the enzymes have also been determined.

Abstract: A method of preparing .varies.-glucan lyase enzymes is described. The method comprises isolating the enzymes from a culture of fungus wherein the culture is substantially free of any other organisms. Also described are the amino acid sequences for the enzymes and their coding sequences.