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US20080003341A1 - Method of Preparing a Dough-Based Product - Google Patents

Method of Preparing a Dough-Based Product Download PDF

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Publication number
US20080003341A1
US20080003341A1 US11/575,644 US57564405A US2008003341A1 US 20080003341 A1 US20080003341 A1 US 20080003341A1 US 57564405 A US57564405 A US 57564405A US 2008003341 A1 US2008003341 A1 US 2008003341A1
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United States
Prior art keywords
polypeptide
amino acid
sucrose
amylase
dough
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Abandoned
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US11/575,644
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English (en)
Inventor
Lars Beier
Esben Friis
Henrik Lundquist
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Novozymes AS
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Novozymes AS
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Assigned to NOVOZYMES A/S reassignment NOVOZYMES A/S ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). Assignors: BEIER, LARS, LUNDQVIST, HENRIK, FRIIS, ESBEN PETER
Publication of US20080003341A1 publication Critical patent/US20080003341A1/en
Abandoned legal-status Critical Current

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    • A—HUMAN NECESSITIES
    • A21—BAKING; EDIBLE DOUGHS
    • A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
    • A21D8/00—Methods for preparing or baking dough
    • A21D8/02—Methods for preparing dough; Treating dough prior to baking
    • A21D8/04—Methods for preparing dough; Treating dough prior to baking treating dough with microorganisms or enzymes
    • A21D8/042—Methods for preparing dough; Treating dough prior to baking treating dough with microorganisms or enzymes with enzymes
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411—Amylases
    • C12N9/2414—Alpha-amylase (3.2.1.1.)
    • C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
    • A—HUMAN NECESSITIES
    • A21—BAKING; EDIBLE DOUGHS
    • A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
    • A21D13/00—Finished or partly finished bakery products
    • A21D13/60—Deep-fried products, e.g. doughnuts
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411—Amylases
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2299/00—Coordinates from 3D structures of peptides, e.g. proteins or enzymes
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01133—Glucan 1,4-alpha-maltohydrolase (3.2.1.133), i.e. maltogenic alpha-amylase

Definitions

  • the present invention comprises a sequence listing.
  • the present invention relates to the use of anti-staling amylases in the preparation of dough or dough-based edible products with a high sucrose content.
  • U.S. Pat. No. 3,026,205 describes a process of producing baked confections and the products resulting therefrom by alpha-amylase.
  • WO 9104669 describes the use of a maltogenic alpha-amylase to retard the staling of baked products such as bread; the maltogenic alpha-amylase described therein is commercially available under the tradename Novamyl® (product of Novozymes A/S).
  • U.S. Pat. No. 6,162,628 describes Novamyl variants and their use for the same purpose. Three-dimensional structures of Novamyl are published in U.S. Pat. No. 6,162,628 and in the Protein Data Bank (available at http://www.rcsb.org/pdb/) with identifiers 1QHO and 1QHP.
  • the inventors have found that a high sucrose content dough (such as cake dough) tends to inhibit the activity of an anti-staling amylases such as Novamyl, making it less effective to prevent the staling of dough-based products with high sucrose content such as cakes. They have found that a good anti-staling effect in cakes can be achieved by using a carefully selected anti-staling amylase with certain properties, and they have identified such amylases.
  • an anti-staling amylases such as Novamyl
  • sucrose may inhibit by binding in the active site. They have found that sucrose docks into the active site of Novamyl differently from the substrate or inhibitor in published models 1QHO and 1QHP, and they have used this finding to design sucrose-tolerant variants.
  • the invention provides a method of preparing dough or a dough-based edible product (e.g. a baked product) by adding a sucrose-tolerant anti-staling amylase. It also provides novel sucrose tolerant variants of a maltogenic alpha-amylase.
  • a maltogenic alpha-amylase (EC 3.2.1.133) having more than 70% identity (particularly more than 80% or 90%, such as at least 95% or 96% or 97% or 98% or 99%) with the Novamyl sequence shown as SEQ ID NO: 1 may be used as the parent enzyme for designing sucrose tolerant variants.
  • Amino acid identity may be calculated as described in U.S. Pat. No. 6,162,628.
  • a 3D structure including a substrate or inhibitor as described in U.S. Pat. No. 6,162,628 or in the Protein Data Bank with the identifier 1QHO or 1QHP may be used.
  • a Novamyl variant may be used, such as a variant described in U.S. Pat. No. 6,162,628 or in this specification, e.g. the variant F188L+D261G+T288P.
  • a 3D structure of a variant may be developed from the Novamyl structure by known methods, e.g. as described in T. L. Blundell et al., Nature, vol. 326, p. 347 ff (26 Mar. 1987); J. Greer, Proteins: Structure, Function and Genetics, 7:317-334 (1990); or Example 1 of WO 9623874.
  • sucrose may inhibit Novamyl by binding in the active site.
  • Docking of sucrose into the active site of Novamyl (using the software GOLD version 2.1.2, Cambridge Crystallographic Data Centre, 12 Union Road, Cambridge, CB2 1EZ, UK and the protein part of the x-ray structure 1QHO.pdb) reveals a specific binding configuration as unique to sucrose.
  • the cartesian coordinates for the sucrose atoms in this binding configuration, using the coordinate system of the x-ray structure 1QHO.pdb are given in FIG. 1 .
  • the activity of a maltogenic alpha-amylase may be determined using an activity assay such as the MANU method.
  • MANU Mealtogenic Amylase Novo Unit
  • One MANU is defined as the amount of enzyme required to release one micro-mole of maltose per minute at a concentration of 10 mg of maltotriose substrate per ml in 0.1 M citrate buffer at pH 5.0, 37° C. for 30 minutes.
  • the amino acid sequence of a maltogenic alpha-amylase may be altered to decrease the sucrose inhibition.
  • the following Novamyl residues are within 4 ⁇ : K44, N86, Y89, H90, Y92, W93, F188, T189, D190, P191, A192, F194, D372, P373, R376.
  • the alteration may be a substitution or deletion of one or more of the selected residues, or one or more residues (particularly 1-4 residues or 5-6 residues) can be inserted adjacent to a selected residue.
  • substitution may be with a smaller or larger residue.
  • a substitution to increase the size of the residue may diminish the space obtained by the docked sucrose molecule thereby preventing the binding of sucrose.
  • substitution may also be such as to eliminate contacts with the sucrose molecule, in particular by moving or removing potential sites of hydrogen bonding or Van der Waals interactions.
  • the substitution may particularly be with another residue of the same type where the type is negative, positive, hydrophobic or hydrophilic.
  • the negative residues are D,E
  • the positive residues are K/R
  • the hydrophobic residues are A, C, F, G, I, L, M, P, V, W, Y
  • the hydrophilic residues are H, N, Q, S, T.
  • substitutions are I15T/S/V/L, R18K, K44R/S/T/Q/N, N86Q/S/T, T87N/Q/S, G88A/S/T, Y89W/F/H, H90W/F/Y/R/K/N/Q/M, W93Y/F/M/E/G/V/T/S, F188H/L/I/T/G/V, D190E/Q/G, A192S/T, F194S/L/Y, L196F, N371K/R/F/Y/Q, D372E/Q/S/T/A and N375S/T/D/E/Q.
  • deletions are deletion of residue 191 or 192.
  • An example of an insertion is Ala inserted between 192 and 193.
  • the polypeptide may include other alterations compared to Novamyl (SEQ ID NO: 1), e.g. alterations to increase the thermostability as described in U.S. Pat. No. 6,162,628.
  • an amino acid substitution is described by use of one-letter codes, e.g. K44R.
  • Slashes are used to indicate alternatives, e.g. K44R/S/T/Q/N to indicate substitution of K44 with R or S etc.
  • P191* indicates a deletion of P191.
  • *192aA indicates insertion of one Ala after A192.
  • Commas are used to indicate multiple alterations in the sequence, e.g. F188L, D261G, T288P to indicate a variant with three substitutions.
  • the amylase for use in high-sucrose dough may be selected so as to have mainly exo-amylase activity. More specifically, the amylase hydrolyzes amylose so that the average molecular weight of the amylose after 0.4-4% hydrolysis is more than 50% (particularly more than 75%) of the molecular weight before the hydrolysis.
  • the amylase may hydrolyze amylose (e.g. wheat amylose or synthetic amylose) so that the average molecular weight of the amylose after 0.4-4% hydrolysis (i.e. between 0.4-4% hydrolysis of the total number of bonds) is more than 50% (particularly more than 75%) of the value before the hydrolysis.
  • amylose e.g. wheat amylose or synthetic amylose
  • the hydrolysis can be conducted in a 1.7% amylose solution by weight at suitable conditions (e.g. 10 minutes at 60° C., pH 5.5), and the molecular weight distribution before and after the hydrolysis can be determined by HPLC.
  • suitable conditions e.g. 10 minutes at 60° C., pH 5.5
  • the test may be carried out as described in C. Christophersen et al., Starch 50 (1), 39-45 (1998).
  • An exo-amylase for use in high-sucrose dough may have a specified sugar tolerance. Compared to its activity in the absence of sucrose, the amylase may have more than 20% activity at 10% sugar, more than 10% activity at 20% sucrose, or more than 4% activity at 40% sucrose.
  • the sugar tolerance may be determined as described in the examples.
  • the exo-amylase may have optimum activity in the pH range 4.5-8.5. It may have sufficient thermostability to retain at least 20% (particularly at least 40%) activity after 30 minutes incubation at 85° C. at pH 5.7 (50 mM Na-acetate, 1 mM CaCl 2 ) without substrate.
  • the exo-amylase may be added to the dough in an amount corresponding to 1-100 mg enzyme protein per kg of flour, particularly 5-50 mg per kg.
  • the exo-amylase may be non-liquefying. This can be determined by letting the exo-amylase act on a 1% wheat starch solution until the reaction is complete, i.e. addition of fresh enzyme causes no further degradation, and analyzing the reaction products, e.g. by HPLC. Typical reaction conditions are e.g. 0.01 mg enzyme per ml starch solution for 48 hours. The exo-amylase is considered non-liquefying if the amount of residual starch after the reaction is at least 20% of the initial amount of starch.
  • the exo-amylase may have maltogenic alpha-amylase activity (EC 3.2.1.133).
  • the exo-amylase may be the amylase described in DK PA 2004 00021, or it may be a Novamyl variant described in this specification.
  • the dough may have a sucrose content above 10% by weight, particularly above 20% or 30%, e.g. 30-40%.
  • the flour content is typically 25-35% by weight of total ingredients.
  • the dough may be made by a conventional cake recipe, typically with cake flour, sugar, fat/oil and eggs as the major ingredients. It may include other conventional ingredients such as emulsifiers, humectants, gums, starch and baking powder. It generally contains such ingredients as soft wheat flour, milk or other liquids, sugar, eggs, chemical leaveners, flavor extracts and spices, as well as others that may or may not include shortening.
  • the dough is generally heat treated, e.g. by baking or deep frying to prepare an edible product such as cakes including pound cake, yellow and white layer cakes, cakes containing chocolate and cocoa products, sponge cakes, angel food cake, fruit cakes and foam-type cakes and doughnuts.
  • an edible product such as cakes including pound cake, yellow and white layer cakes, cakes containing chocolate and cocoa products, sponge cakes, angel food cake, fruit cakes and foam-type cakes and doughnuts.
  • amylases were tested for thermostability and sugar tolerance: bacterial alpha-amylase from B. amyloliquefaciens (BANTM, product of Novozymes A/S), fungal alpha-amylase from A. oryzae (Fungamyl®, product of Novozymes A/S), maltogenic alpha-amylase having the sequence of SEQ ID NO: 1 (Novamyl®, product of Novozymes A/S), a Novamyl variant having SEQ ID NO: 1 with the substitutions F188L+D261G+T288P, and bacterial alpha-amylase from B. licheniformis (Termamyl®, product of Novozymes A/S).
  • amylase activity was measured after 0, 15, 30 and 60 minutes heat treatment. The results are expressed as residual activity in % of the initial activity: 0 15 30 60 BAN 100 3 1 0 Fungamyl 100 0 0 0 Novamyl 100 51 29 13 Novamyl variant 100 64 48 54 Termamyl 100 100 71 85
  • Sponge cakes were made with addition of amylase as follows: BAN (0.83. 8.3 or 83 mg/kg flour), Novamyl (1.3 or 13 mg/kg flour) or the Novamyl variant used in Example 1 (1, 10 or 100 mg/kg flour). A control cake was made without amylase.
  • the cakes were baked according to the High Ratio Sponge Sandwich Cake (HRSSC) method. After baking, the cakes were cooled down for 60-120 minutes, and the cakes were stored at room temperature in sealed plastic bags filled with nitrogen until analysis. The cakes were evaluated on day 1, 3, 7 or 23.
  • HRSSC High Ratio Sponge Sandwich Cake
  • a small sensory evaluation of softness and moistness was performed on day 13 for the 3 cakes with the Novamyl variant and the control cake.
  • the cakes were evaluated regarding three parameters; Firmness, Moistness and preferability.
  • the control was the firmest, driest and least preferred.
  • Cakes were baked according to the High ratio unit cake (HRUC) method. After baking, the cakes were cooled down for 60-120 minutes, and the cakes were stored at room temperature in sealed plastic bags filled with Nitrogen until analysis. The cakes were evaluated on day 7, 20 and 34 by the same methods as in the previous example.
  • HRUC High ratio unit cake
  • the Novamyl variant and BAN were able to keep the cake more moist than the control. This increase in mobility of the free water could partly be explained by the cakes with BAN and the Novamyl variant being able to retain the moisture content.
  • Sponge cakes were made with addition of the amylase of DK PA 2004 00021 at dosages 0.5, 1, 2, 5 and 20 mg/kg flour and a control cake without amylase.
  • Texture and NMR was measured on day 1, 7 and 13.
  • the addition of the amylase reduced the increase in firmness, especially at the highest dosage.
  • the amylase also had a beneficial effect on the mobility of water which was correlated with the moistness of the cake.
  • a blind sensory ranking evaluation performed on day 14 showed a ranking according to the dosage, the higher dosage the more soft and moist cake. The most preferred cake was the one with the highest dosage.
  • the ingredients were scaled into a mixing bowl and mixed using an industrial mixer (e.g. Bj ⁇ rn AR 5 A Varimixer) with a suitable paddle speed. 300 g of the dough was poured into forms. The cakes are baked in a suitable oven (e.g. Sveba Dahlin deck oven) for 45 min. at 180° C. The cakes were allowed to cool down at room temperature for 1 hour.
  • an industrial mixer e.g. Bj ⁇ rn AR 5 A Varimixer
  • suitable paddle speed 300 g of the dough was poured into forms.
  • the cakes are baked in a suitable oven (e.g. Sveba Dahlin deck oven) for 45 min. at 180° C.
  • the cakes were allowed to cool down at room temperature for 1 hour.
  • the volume of the cakes was determined when the cakes had cooled down using the rape seed displacement method.
  • the cakes were packed under nitrogen in sealed plastic bags and stored at room temperature until analysis.
  • TPA Texture profile analysis

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US11/575,644 2004-09-24 2005-09-23 Method of Preparing a Dough-Based Product Abandoned US20080003341A1 (en)

Applications Claiming Priority (3)

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DKPA200401458 2004-09-24
DKPA200401458 2004-09-24
PCT/DK2005/000602 WO2006032281A2 (fr) 2004-09-24 2005-09-23 Procede de preparation d'un produit a base de pate

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US12/964,189 Abandoned US20110305795A1 (en) 2004-09-24 2010-12-09 Method of preparing a dough-based product
US13/742,998 Expired - Lifetime US9226510B2 (en) 2004-09-24 2013-01-16 Method of preparing a dough-based product
US14/955,490 Expired - Lifetime US9439442B2 (en) 2004-09-24 2015-12-01 Method of preparing a dough-based product

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US13/742,998 Expired - Lifetime US9226510B2 (en) 2004-09-24 2013-01-16 Method of preparing a dough-based product
US14/955,490 Expired - Lifetime US9439442B2 (en) 2004-09-24 2015-12-01 Method of preparing a dough-based product

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US (4) US20080003341A1 (fr)
EP (1) EP1794291B1 (fr)
AU (1) AU2005287737B2 (fr)
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DK (1) DK1794291T3 (fr)
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US20120225164A1 (en) * 2009-11-13 2012-09-06 Novozymes A/S Brewing method
US20160120614A1 (en) * 2014-10-08 2016-05-05 Northeast Scientific, Inc. Displacement control wire device and method
JP2019198319A (ja) * 2018-05-09 2019-11-21 ミヨシ油脂株式会社 製菓練り込み用油脂組成物とそれを用いた製菓
US10631547B2 (en) * 2014-09-29 2020-04-28 Puratos Nv Cake batters
US11999928B2 (en) 2009-11-13 2024-06-04 Novozymes A/S Brewing method

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DK2164958T3 (en) * 2007-06-07 2014-11-24 Novozymes As A process for preparing a dough-based product
AU2013204951B2 (en) * 2007-06-07 2014-12-04 Novozymes A/S Method of preparing a dough-based product
CN102665425A (zh) 2009-09-30 2012-09-12 诺维信公司 馒头制备方法和馒头改进组合物
EP2579727B1 (fr) 2010-06-11 2018-08-08 Novozymes A/S Correction enzymatique de la farine
EP2486799A1 (fr) 2011-02-14 2012-08-15 DSM IP Assets B.V. Procédé pour produire des gâteaux comprenant une enzyme lipolytique et une alpha-amylase
WO2012130969A1 (fr) 2011-03-29 2012-10-04 Novozymes A/S Procédé de production d'un produit de boulangerie-pâtisserie
DK2840900T3 (da) * 2012-04-25 2019-09-09 Novozymes As Fremgangsmåde til bagning
JP6325535B2 (ja) 2012-06-27 2018-05-16 ノボザイムス アクティーゼルスカブ 米の調理方法
US9301533B2 (en) 2013-03-01 2016-04-05 Dsm Ip Assets B.V. Alpha-amylase variants
AU2017295412B2 (en) 2016-07-15 2022-02-03 Novozymes A/S Improving the rollability of flat breads
US11051520B2 (en) 2017-02-20 2021-07-06 Novozymes A/S Lipolytic enzyme for use in baking
EP3641550B1 (fr) 2017-06-22 2021-05-05 Novozymes A/S Procede pour ameliorer l'extensibilite de la pate a l'aide de la gamma glutamyl transpeptidase
CN111935981B (zh) 2018-04-05 2024-06-14 帝斯曼知识产权资产管理有限公司 变体麦芽糖α-淀粉酶
EP3780960B1 (fr) * 2018-04-19 2026-01-14 Novozymes A/S Procede d'amelioration de la fraicheur de pains plats par combinaison de variants d'alpha-amylase maltogene et de prémélange de pâte à pain plat
CA3101914A1 (fr) 2018-06-04 2019-12-12 Novozymes A/S Article enzymatique solide destine a etre utilise dans la cuisson
US12171240B2 (en) 2018-06-12 2024-12-24 Novozymes A/S Less added sugar in baked products
CN114929022A (zh) 2019-12-09 2022-08-19 诺维信公司 烘焙添加剂
CN113558081A (zh) 2020-04-29 2021-10-29 诺维信公司 一种酶法减少烘焙产品中油脂使用量的方法
AU2021372822A1 (en) 2020-11-02 2023-06-01 Novozymes A/S Baked and par-baked products with thermostable amg variants from penicillium
CA3268687A1 (fr) 2022-10-24 2024-05-02 Novozymes A/S Procédé de cuisson pour pain enrichi en protéine pulsée utilisant de l'amyloglucosidase thermostable (ec 3.2.1.3)
CN120091760A (zh) 2022-10-24 2025-06-03 诺维信公司 使用热稳定AMG变体和α-淀粉酶的烘焙方法
WO2024089126A1 (fr) 2022-10-28 2024-05-02 Novozymes A/S Procédé d'obtention d'un ingrédient alimentaire d'origine végétale
AU2022489922A1 (en) 2022-11-30 2025-05-22 Novozymes A/S Baking at low-ph with thermostable glucoamylase variants
WO2024243330A1 (fr) 2023-05-22 2024-11-28 Caravan Ingredients Inc. Amplificateur de produits de boulangerie et ses procédés de fabrication et d'utilisation
AU2024321426A1 (en) 2023-08-09 2026-01-29 Novozymes A/S Methods for obtaining a plant-based food ingredient

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AU2005287737A1 (en) 2006-03-30
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WO2006032281A2 (fr) 2006-03-30
CA2610683C (fr) 2015-12-22
DK1794291T3 (da) 2013-03-04
US9226510B2 (en) 2016-01-05
ES2399341T3 (es) 2013-03-27
US9439442B2 (en) 2016-09-13
WO2006032281A3 (fr) 2006-12-28
US20160081357A1 (en) 2016-03-24
US20110305795A1 (en) 2011-12-15
CA2610683A1 (fr) 2006-03-30
US20130136823A1 (en) 2013-05-30

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