A process of enzymatic degumming edible oils, comprising treating edible oil with a lipid acyltransferase so as to transfer an acyl group from a major part of the phospholipid to one or more acyl acceptors, wherein the acyl acceptor may be any compound comprising a hydroxyl group. In one embodiment
A process of enzymatic degumming edible oils, comprising treating edible oil with a lipid acyltransferase so as to transfer an acyl group from a major part of the phospholipid to one or more acyl acceptors, wherein the acyl acceptor may be any compound comprising a hydroxyl group. In one embodiment preferably the acyl acceptor is water and in another embodiment preferably the acyl acceptor is one or more sterols and/or stanols. When the acyl acceptor is a stanol and/or sterol, one or more sterol esters and/or stanol esters are produced. The lipid acyltransferase for use in the process of the present invention may comprise one or more of the following amino acid sequences: SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, or SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 36, SEQ ID NO: 38, SEQ ID NO: 40, SEQ ID NO: 41, SEQ ID NO: 45, SEQ ID NO: 47, SEQ ID NO: 50 or an amino acid sequence which has 75% or more identity thereto. A novel lipid acyltransferase comprising the amino acid sequence shown as SEQ ID NO: 16 is also taught.
대표청구항▼
1. A process of enzymatic degumming an edible oil, comprising treating the edible oil with a lipid acyltransferase, wherein the lipid acyltransferase:(a) transfers an acyl group from a phospholipid to one or more acyl acceptors selected from sterol and stanol to form an ester;(b) comprises an amino
1. A process of enzymatic degumming an edible oil, comprising treating the edible oil with a lipid acyltransferase, wherein the lipid acyltransferase:(a) transfers an acyl group from a phospholipid to one or more acyl acceptors selected from sterol and stanol to form an ester;(b) comprises an amino acid sequence motif GDSX, wherein X is an amino acid residue selected from L, A, V, I, F, Y, H, Q, T, N, M and S;(c) when aligned to either SEQ ID NO: 2 or SEQ ID NO: 37 has a GANDY block; and(d) has at least 5% acyltransferase activity when reacted with a substrate, wherein the substrate is soya bean oil supplemented with 1% plant sterol and 2% phosphatidylcholine, wherein: (i) the substrate to which no enzyme has been added is a control;(ii) in an enzymatic reaction with the substrate, lipid material from the reaction and the control are analyzed; and(iii) acyltransferase activity is calculated as a percentage of total enzymatic activity using the formula: (Δ×100)/((Δ+Δ % fatty acid)/Mv fatty acid),wherein:Δ % fatty acid=% fatty acid(enzyme)−% fatty acid(control);Mv fatty acid=average molecular weight of the fatty acids; andΔ=Δ % sterol ester/Mv sterol ester, wherein:Δ % sterol ester=% sterol/stanol ester(enzyme)−% sterol/stanol ester(control); andMv sterol ester=average molecular weight of the sterol/stanol esters. 2. A process according to claim 1, wherein a sterol ester, a stanol ester, or both a sterol ester and a stanol ester is formed. 3. A process according to claim 1, wherein the acyl acceptor is a sterol. 4. A process according to claim 1, wherein the phospholipid is a lecithin. 5. A process according to claim 1, wherein the lipid acyltransferase transfers the acyl group from a lipid to one or more acyl acceptors selected from a carbohydrate, a protein, a protein subunit, and glycerol. 6. A process according to claim 1, wherein the lipid acyltransferase is a natural lipid acyltransferase. 7. A process according to claim 1, wherein the lipid acyltransferase is a variant lipid acyltransferase. 8. A process according to claim 1 wherein, the lipid acyltransferase is obtained from an organism selected from: Aeromonas, Streptomyces, Saccharomyces, Lactococcus, Mycobacterium, Streptococcus, Lactobacillus, Desulfitobacterium, Bacillus, Campylobacter, Vibrionaceae, Xylella, Sulfolobus, Aspergillus, Schizosaccharomyces, Listeria, Neisseria, Mesorhizobium, Ralstonia, Xanthomonas, Candida, Thermobifida and Corynebacterium. 9. A process according to claim 1, wherein the lipid acyltransferase is obtained from an organism selected from: Aeromonas hydrophila, Aeromonas salmonicida, Striptomyces coelicolor, Streptomyces rimosus, Streptomyces thermosacchari, Streptomyces avermitilis, Mycobacterium, Streptococcus pyogenes, Lactococcus lactis, Streptococcus pyogenes, Streptococcus thermophilus, Lactobacillus helveticus, Desulfitobacterium dehalogenans, Bacillus sp, Campylobacter jejuni, Vibrionaceae, Xylella fastidiosa, Sulfolobus solfataricus, Saccharomyces cerevisiae, Aspergillus terreus, Schizosaccharomyces pombe, Listeria innocua, Listeria monocytogenes, Neisseria meningitidis, Mesorhizobium loti, Ralstonia solanacearum, Xanthomonas campestris, Xanthomonas axonopodis, Candida parapsilosis, Thermobifida fusca and Corynebacterium efficiens. 10. A process according to claim 1, wherein the X of the GDSX motif is L. 11. A process according to claim 1, wherein the lipid acyltransferase is selected from: SEQ ID No. 1, SEQ ID No. 3, SEQ ID No. 4, SEQ ID No. 5, SEQ ID No. 6, SEQ ID No. 7, SEQ ID No. 8, SEQ ID No. 9, SEQ ID No. 10, SEQ ID No. 11, SEQ ID No. 12, SEQ ID No. 13, SEQ ID No. 14, or SEQ ID No. 15, SEQ ID No. 16, SEQ ID No. 17, SEQ ID No. 18, SEQ ID No. 36, SEQ ID No. 38, SEQ ID No. 40, SEQ ID No. 41, SEQ ID No 45, SEQ ID No. 47, SEQ ID No. 50, and an amino acid sequence which has 95% or more identity thereto. 12. A process according to claim 1 wherein the lipid acyltransferase has the amino acid sequence shown as SEQ ID No. 16, or an amino acid sequence which has 95% or more homology thereto. 13. A process according to claim 12, wherein the lipid acyltransferase has the amino acid sequence shown as SEQ ID No. 16. 14. A process according to claim 7, wherein the variant lipid acyltransferase comprises the amino acid sequence motif GDSX, wherein: X is an amino acid residue selected from L, A, V, I, F, Y, H, Q, T, N, M and S; andthe variant lipid acyltransferase comprises one or more amino acid modifications compared with a parent sequence at any one or more of the amino acid residues defined in set 2 or set 4 or set 6 or set 7. 15. A process according to claim 7, wherein the variant lipid acyltransferase has the amino acid sequence shown as SEQ ID No. 16, or an amino acid sequence with 95% or more homology thereto. 16. A process according to claim 15, wherein the variant lipid acyltransferase has the amino acid sequence shown as SEQ ID No. 16. 17. A process according to claim 1, wherein there is less than 1% water in the edible oil. 18. A process according to claim 17, wherein there is less than 0.5% water in the edible oil. 19. A process according to claim 18, wherein there is less than 0.1% water in the edible oil. 20. A process according to claim 1, further comprising removing by filtration the lysophospholipids produced by action of the lipid acyltransferase.
Inoue Seijiro (Machida JPX) Ota Shigenori (Komae JPX), Bread or other cereal-based food improver composition involving the addition of phospholipase A to the flour.
Derez Frank G. H. (Halle BEX) de Sadeleer Jos W. G. C. (Kessel Lo BEX) Reeve Alan L. (Leefdaal BEX), Carbohydrate refining process and novel enzyme compositions suitable for use therein.
Artiss Joseph D. (2761 Avondale Court Windsor ; Ontario MI CAX N9E 1X1) Zak Bennie (6692 Maple Lakes Dr. West Bloomfield MI 48033), Composition for reducing turbidity in samples of biological fluids.
Brown Peter H. (Morton Grove IL) Carvallo Federico D. (Wheeling IL) Dinwoodie Robert C. (Glenview IL) Dueber Michael T. (Glenview IL) Hayashi David K. (Chicago IL) Krishnamurthy R. G. (Glenview IL) M, Enzymatic method for preparing transesterified oils.
Aalrust Erik (Seeheim-Jugenheim DEX) Beyer Wolfgang (Hermannsburg DEX) Ottofrickenstein Hans (Darmstadt-Eberstadt DEX) Penk Georg (Bad Vilbel DEX) Plainer Hermann (Reinheim DEX) Reiner Roland (Darmst, Enzymatic treatment of edible oils.
Van Den Ouweland Godefridus (Confignon CHX) Escher Sina Dorothea (Confignon CHX) Benzi Franois (Geneva CHX) Vanrietvelde Claude (St-Julien-en-Genevois FRX), Flavoring composition and process.
Terada Osamu (Machida JPX) Uwajima Takayuki (Machida JPX) Mihara Akira (Machida JPX) Aisaka Kazuo (Machida JPX) Akita Hiroko (Yokohama JPX) Nagai Toshiaki (Sunto JPX) Shimizu Yoshiaki (Sunto JPX), Glycerol oxidase and process for the production thereof and method for the quantitative determination of glycerol by gly.
Loffler Fridolin,DEX ; Nguyen Quoc Khanh,DEX ; Schuster Erwin,DEX ; Sprossler Bruno,DEX ; Thomas Lutz ; Wolf Sabine,DEX, Lysophospholipase produced from aspergillus by recombinant methods.
Gauhl Helmgard (Tutzing DEX) Seidel Hans (Tutzing DEX) Lang Gunter (Tutzing DEX) Rder Albert (Seeshaupt DEX) Ziegenhorn Joachim (Starnberg DEX), Method and reagent for the determination of glycerin.
Søe, Jorn Borch; Poulsen, Charlotte Horsmans; Rasmussen, Preben; Madrid, Susan Mampusti; Zargahi, Masoud R., Method for preparing flour doughs and products made from such doughs using lipase.
Pedersen Sven,DKX ; Larsen Anne M.o slashed.rkeberg,DKX ; Aasmul Per,DKX, Method of enzyme immobilization on a particulate silica carrier for synthesis inorganic media.
J?rn Borch S?e DK; Charlotte Horsmans Poulsen DK; Pernille Bak H?strup DK, Method of improving the properties of a flour dough, a flour dough improving composition and improved food products.
Olsen, Torkil Steenholt; Povlsen, Inge Lise; Soe, Jorn Borch; Poulsen, Charlotte Horsmans; Hostrup, Pernille Bak, Method of improving the properties of a flour dough, a flour dough improving composition and improved food products.
Søe, Jørn Borch; Poulsen, Charlotte Horsmans; Høstrup, Pernille Bak, Method of improving the properties of a flour dough, a flour dough improving composition and improved food products.
Hattori Atsushi (Tokyo JPX) Uchida Noriyoshi (Tokyo JPX) Kitaoka Masahiro (Tokyo JPX), Phospholipase A1, process for its preparation and the use thereof.
Berka, Randy M.; Rey, Michael W.; Byun, Tony; Itami, Ryoko; Tsutsumi, Noriko; Klotz, Alan, Polypeptides having phospholipase activity and nucleic acids encoding same.
Kurashige Jun (Kawasaki JPX) Matsuzaki Narihide (Kawasaki JPX) Mase Tamio (Nishikasugai JPX) Yamaguchi Shotaro (Nishikasugai JPX), Process for modifying fats and oils.
Boel Esper,DKX ; Christensen Tove,DKX ; Woldike Helle Fabbicius,DKX ; Huge-Jensen Ida Birgitte,DKX, Process for the production of protein products in aspergillus.
Reubi, Jean-Claude; Breeman, Wout A.; Srinivasan, Ananthachari, Radiolabeled peptides for the diagnosis and treatment of breast and prostate tumors and metastases of such tumors.
Nakanishi Yuji (Aichi JPX) Kurono Yoshiaki (Aichi JPX) Koide Yoshinao (Aichi JPX) Beppu Teruhiko (Tokyo JPX), Recombinant DNA, bacterium of the genus Pseudomonas containing it, and process for preparing lipase by using it.
Cabilly Shmuel (Monrovia CA) Heyneker Herbert L. (Burlingame CA) Holmes William E. (Pacifica CA) Riggs Arthur D. (La Verne CA) Wetzel Ronald B. (San Francisco CA), Recombinant immunoglobin preparations.
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