EP4608148A1 - Procédé de cuisson pour pain enrichi en protéine pulsée utilisant de l'amyloglucosidase thermostable (ec 3.2.1.3) - Google Patents

Procédé de cuisson pour pain enrichi en protéine pulsée utilisant de l'amyloglucosidase thermostable (ec 3.2.1.3)

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Publication number
EP4608148A1
EP4608148A1 EP22829700.8A EP22829700A EP4608148A1 EP 4608148 A1 EP4608148 A1 EP 4608148A1 EP 22829700 A EP22829700 A EP 22829700A EP 4608148 A1 EP4608148 A1 EP 4608148A1
Authority
EP
European Patent Office
Prior art keywords
seq
amino acid
dough
enzyme
flour
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Pending
Application number
EP22829700.8A
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German (de)
English (en)
Inventor
Henrik Lundkvist
Camilla VARMING
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novozymes AS
Original Assignee
Novozymes AS
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Filing date
Publication date
Application filed by Novozymes AS filed Critical Novozymes AS
Publication of EP4608148A1 publication Critical patent/EP4608148A1/fr
Pending legal-status Critical Current

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Classifications

    • 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
    • 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
    • A21D13/04—Products made from materials other than rye or wheat flour
    • A21D13/045—Products made from materials other than rye or wheat flour from leguminous plants
    • 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
    • A21D13/06—Products with modified nutritive value, e.g. with modified starch content
    • A21D13/062—Products with modified nutritive value, e.g. with modified starch content with modified sugar content; Sugar-free products
    • 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
    • A21D13/06—Products with modified nutritive value, e.g. with modified starch content
    • A21D13/064—Products with modified nutritive value, e.g. with modified starch content with modified protein content
    • A—HUMAN NECESSITIES
    • A21—BAKING; EDIBLE DOUGHS
    • A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
    • A21D2/00—Treatment of flour or dough by adding materials thereto before or during baking
    • A21D2/08—Treatment of flour or dough by adding materials thereto before or during baking by adding organic substances
    • A21D2/24—Organic nitrogen compounds
    • A21D2/26—Proteins
    • A21D2/264—Vegetable proteins
    • A—HUMAN NECESSITIES
    • A21—BAKING; EDIBLE DOUGHS
    • A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
    • A21D2/00—Treatment of flour or dough by adding materials thereto before or during baking
    • A21D2/08—Treatment of flour or dough by adding materials thereto before or during baking by adding organic substances
    • A21D2/24—Organic nitrogen compounds
    • A21D2/26—Proteins
    • A21D2/264—Vegetable proteins
    • A21D2/266—Vegetable proteins from leguminous or other vegetable seeds; from press-cake or oil bearing seeds
    • A—HUMAN NECESSITIES
    • A21—BAKING; EDIBLE DOUGHS
    • A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
    • A21D2/00—Treatment of flour or dough by adding materials thereto before or during baking
    • A21D2/08—Treatment of flour or dough by adding materials thereto before or during baking by adding organic substances
    • A21D2/24—Organic nitrogen compounds
    • A21D2/26—Proteins
    • A21D2/267—Microbial proteins
    • 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)
    • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
    • C12N9/18—Carboxylic ester hydrolases (3.1.1)
    • C12N9/20—Triglyceride splitting, e.g. by means of lipase
    • 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.)
    • 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
    • C12N9/2428—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
    • 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)
    • C12Y302/01003—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
    • C12R2001/00—Microorganisms ; Processes using microorganisms
    • C12R2001/645—Fungi ; Processes using fungi
    • C12R2001/80—Penicillium
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y301/00—Hydrolases acting on ester bonds (3.1)
    • C12Y301/01—Carboxylic ester hydrolases (3.1.1)
    • C12Y301/01004—Phospholipase A2 (3.1.1.4)
    • 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)
    • C12Y302/01001—Alpha-amylase (3.2.1.1)

Definitions

  • the invention relates to methods of producing a baked or partially baked product comprising providing a dough comprising added pulse and/or legume protein and a mature thermostable variant of a parent glucoamylase at least 70% identical to SEQ ID NO:1 , SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8 or SEQ ID NQ:10; and baking or partially baking the dough to produce the baked or partially baked product.
  • Par-baking is a technique where a bread or another dough product is partially (i.e. “par”) baked and then typically cooled or frozen for storage.
  • the cooled or frozen par-baked product is baked at normal baking temperatures for typically 5 to 15 minutes; the resulting type of baked product is frequently referred to as “bake-off”.
  • WO 2021/239267 discloses methods of producing baked or partially baked edible products from dough comprising added pulse and/or legume protein and at least one added lipase enzyme, wherein at least 2% (w/w) of the total flour content is added pulse and/or legume protein.
  • thermostable variants of certain glucoamylases showed improved performance in baking with added pulse and/or legume protein.
  • One improved performance of the thermostable variants was that they increased the sweetness or sweet taste of the product, which allowed a reduction in the amount of added sugar in traditional recipes and also to some extent was able to mask otherwise bitter flavours from the added pulse and/or legume protein.
  • the invention relates to methods of producing a baked or partially baked product comprising providing a dough comprising added pulse and/or legume protein and a mature thermostable variant of a parent glucoamylase at least 70% identical to SEQ ID NO:1 , SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8 or SEQ ID NQ:10; and baking or partially baking the dough to produce the baked or partially baked product.
  • the mature thermostable variant of a parent glucoamylase of the invention is at least 71 % identical to SEQ ID NO:1 , SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8 or SEQ ID NO: 10, e.g. at least 72%, e.g. at least 73%, e.g. at least 74%, e.g. at least 75%, e.g. at least 76%, e.g. at least 77%, e.g. at least 78%, e.g. at least 79%, e.g., at least 80%, e.g. at least 81%, e.g. at least 82%, e.g. at least 83%, e.g.
  • At least 84% e.g., at least 85%, e.g. at least 86%, e.g. at least 87%, e.g. at least 88%, e.g. at least 89%, e.g., at least 90%, e.g., at least 91%, e.g., at least 92%, e.g., at least 93%, e.g., at least 94%, e.g., at least 95%, e.g.
  • Figure 1 shows a multiple alignment of the amino acid sequences of the mature proteins of:
  • Legumes are plants in the Fabaceae family (or Leguminosae), or the fruit or seed of such a plant (also called a pulse, especially in the mature, dry condition).
  • Well-known legumes include alfalfa, clover, beans, peas, chickpeas, lentils, lupins, mesquite, carob, soybeans, peanuts, and tamarind.
  • Legumes produce a botanically unique type of fruit - a simple dry fruit that develops from a simple carpel and usually dehisces (opens along a seam) on two sides.
  • Pulse The United Nations Food and Agriculture Organization (FAO) recognizes 11 types of pulses: dry beans, dry broad beans, dry peas, chickpeas, cow peas, pigeon peas, lentils, Bambara beans, vetches, lupins and pulses NES (/.e. minor pulses, including: Lablab, hyacinth bean (Lablab purpureus), Jack bean (Canavalia ensiformis), sword bean (Canavalia gladiata), Winged bean (Psophocarpus tetragonolobus), Velvet bean, cowitch (Mucuna pruriens var. utilis), Yam bean (Pachyrhizus erosus).
  • FEO Food and Agriculture Organization
  • Deflavoured pulse and/or legume flour or protein in the context of the instant invention, the term ‘deflavoured’ means that the flour or protein component has been processed to reduce off-flavour, e.g., bitterness.
  • Galactolipase activity EC 3.1.1.26
  • DGDG digalactosyl diglyceride
  • Sequence identity The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity”.
  • amino acid changes may be of a minor nature, that is conservative amino acid substitutions or insertions that do not significantly affect the folding and/or activity of the protein; small deletions, typically of 1-30 amino acids; small amino- or carboxyl-terminal extensions, such as an aminoterminal methionine residue; a small linker peptide of up to 20-25 residues; or a small extension that facilitates purification by changing net charge or another function, such as a poly-histidine tract, an antigenic epitope, or a binding domain.
  • conservative substitutions are within the groups of basic amino acids (arginine, lysine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine and valine), aromatic amino acids (phenylalanine, tryptophan and tyrosine), and small amino acids (glycine, alanine, serine, threonine and methionine).
  • Amino acid substitutions that do not generally alter specific activity are known in the art and are described, for example, by H. Neurath and R.L. Hill, 1979, In, The Proteins, Academic Press, New York.
  • thermostability improvement (Td) in °C is a measure of how much the variants have improved in thermostability over their parent glucoamylase under the same conditions, determined as exemplified herein.
  • Improved crumb firmness of the baked product is defined herein as the property of a baked product that is more easily compressed compared to a baked product wherein the enzyme solution according to the invention is not added to the dough.
  • the crumb firmness is evaluated either empirically by the skilled test baker/sensory panel or measured by the use of a texture analyzer (e.g., TAXT2 or TA-XT Plus from Stable Micro Systems Ltd, Surrey, UK) as known in the art.
  • a texture analyzer e.g., TAXT2 or TA-XT Plus from Stable Micro Systems Ltd, Surrey, UK
  • Improved flavor of the baked product is evaluated by a trained test panel and/or chemical analysis (e.g., headspace GC-MS analysis). Improved flavor of the baked product comprises the reduction of off-flavor(s) of the baked product.
  • Improved anti-staling of the baked product is defined herein as the properties of a baked product that have a reduced rate of deterioration of quality parameters, e.g., softness and/or elasticity, during storage.
  • volume of the baked product is defined herein as the measure of the volume of a given loaf of bread. The volume may be determined by the rape seed displacement method.
  • the invention relates to doughs for baked- or par-baked products, said doughs comprising added pulse and/or legume protein.
  • the term "added” is defined herein as adding the proteins and/or enzymes according to the invention to the dough, to any ingredient from which the dough is to be made, and/or to any mixture of dough ingredients from which the dough is to be made.
  • the proteins and/or enzymes may be added in any step of the dough preparation and may be added in one, two or more steps. They may be added to the ingredients of dough that may be kneaded and processed as known in the art for baked and/or par-baked products.
  • an effective amount is defined herein as an amount of an enzyme composition according to the invention that is sufficient for providing a measurable effect on at least one property of interest of the dough and/or baked product.
  • batter is defined herein as a mixture of flour and other baking ingredients firm enough to knead or roll.
  • batters are encompassed in the term “dough”; preferably the dough of the instant invention comprises wheat flour.
  • the dough ingredients comprise wheat flour; preferably 2% (w/w) or more of the total flour content is wheat flour; preferably 4% (w/w) or more of the total flour content is wheat flour, preferably at least 6%, at least 8%, at least 10%, at least 15 %, at least 20%, at least 25%, at least 30%, at least 35 %, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, or preferably at least 95% (w/w) of the flour is wheat flour.
  • the dough of the invention may comprise flour derived from any cereal grain or other sources, including wheat, emmer, spelt, einkorn, barley, rye, oat, corn, sorghum, rice, millet, amaranth, quinoa, cassava, and any combination thereof.
  • the pulse and/or legume protein is added to the dough in the form of pulse and/or legume flour, processed pulse and/or legume flour, deflavoured pulse and/or legume flour, or protein concentrate and/or isolate made essentially from pulse and/or legume flour; preferably the added pulse and/or legume protein comprises lentil protein, chickpea protein, pea protein and/or faba bean protein, or a protein concentrate and/or isolate thereof.
  • a preferred embodiment relates to the dough according to the first aspect, wherein at least 4% (w/w) of the total flour content is added pulse and/or legume protein, preferably at least 6% (w/w) of the total flour content is added pulse and/or legume protein, more preferably at least 8% (w/w) of the total flour content is added pulse and/or legume protein, even more preferably at least 10% (w/w) of the total flour content is added pulse and/or legume protein, most preferably, at least 12% (w/w) of the total flour content is added pulse and/or legume protein
  • the dough of the invention also comprises gluten.
  • the dough may also comprise other conventional dough ingredients, e.g., proteins, such as milk powder, gluten, source of dietary fiber (such as wheat, oat bran, beta-glucan and/or inulin), and eggs (either whole eggs, egg yolks, or egg whites); an oxidant such as ascorbic acid, potassium bromate, potassium iodate, azodicarbonamide (ADA) or ammonium persulfate; an amino acid such as L-cysteine; a sugar; a salt such as sodium chloride, calcium acetate, sodium sulfate, or calcium sulfate, and/or an emulsifier.
  • proteins such as milk powder, gluten, source of dietary fiber (such as wheat, oat bran, beta-glucan and/or inulin), and eggs (either whole eggs, egg yolks, or egg whites)
  • an oxidant such as ascorbic acid, potassium bromate, potassium iodate, azodicarbonamide (ADA) or ammonium
  • the dough of the invention also comprises gluten.
  • the dough may comprise fat (triglyceride) such as granulated fat or oil.
  • the dough of the invention is normally a leavened dough or a dough to be subjected to leavening.
  • the dough may be leavened in various ways, such as by adding chemical leavening agents, e.g., baking powder, sodium bicarbonate, or by adding a leaven (fermenting dough), but it is preferred to leaven the dough by adding a suitable yeast culture, such as a culture of Saccharomyces cerevisiae (baker's yeast), e.g., a commercially available strain of S. cerevisiae.
  • the doughs of the invention may comprise at least one added lipase enzyme, preferably a lipase and/or a phospholipase, preferably a mature lipase and/or mature phospholipase.
  • the at least one added lipase enzyme comprises a mature lipase having amino acid sequence at least 70% identical to one or more of the sequences shown in SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20 and SEQ ID NO: 21 ; preferably at least 75% identical, at least 80%, 85%, 90%, 92%, 94%, 96%, 98% or preferably at least 99% identical to one or more of the sequences shown in SEQ I D NO: 17, SEQ I D NO: 18, SEQ I D NO: 19, SEQ I D NO: 20 and SEQ ID NO: 21.
  • the at least one added lipase enzyme is added in an amount in the range of 0 to 100 mg enzyme protein/kg flour; preferably in the range of 0 to 50 mg enzyme protein/kg flour; more preferably in an amount in the range of 0 to 25 mg enzyme protein/kg flour; even more preferably in an amount in the range of 0 to 10 mg enzyme protein/kg flour; still more preferably in an amount in the range of 0 to 5 mg enzyme protein/kg flour; and most preferably in an amount in the range of 0 to 2,5 mg enzyme protein/kg flour.
  • the dough of the first aspect also comprises at least one additional added enzyme, preferably at least one mature alpha-amylase, more preferably a mature maltogenic alpha-amylase; preferably a mature maltogenic alpha-amylase from Bacillus stearothermophilus', more preferably a mature maltogenic alpha-amylase having an amino acid sequence at least 70% identical to that of SEQ ID NO:6, preferably at least 75% identical, at least 80%, 85%, 90%, 92%, 94%, 96%, 98% or preferably at least 99% identical to that of SEQ ID NO:11.
  • at least one additional added enzyme preferably at least one mature alpha-amylase, more preferably a mature maltogenic alpha-amylase; preferably a mature maltogenic alpha-amylase from Bacillus stearothermophilus', more preferably a mature maltogenic alpha-amylase having an amino acid sequence at least 70% identical to that of SEQ ID NO:6, preferably at least 75% identical
  • the mature maltogenic alpha-amylase is added in an amount in the range of O to 10.000 MANU/kg flour; preferably in the range of 0 to 7.500 MANU/kg flour; preferably in the range of 0 to 5.000 MANU/kg flour.
  • the at least one additional added enzyme comprises a mature alpha amylase; preferably a mature fungal alpha amylase; more preferably a mature alpha amylase from Aspergillus oryzae preferably the additional mature alpha-amylase is added in an amount in the range of 0 to 1.000 FAll/kg flour; preferably in the range of 0 to 500 FAll/kg flour; more preferably in the range of 0 to 100 FAll/kg flour; even more preferably in the range of 0 to 50 FAll/kg flour; and most preferably in the range of 0 to 25 FAll/kg flour.
  • the dough of the first aspect also comprises at least one additional added enzyme comprises at least one mature xylanase, preferably a GH5, a GH8 and/or a GH11 xylanase.
  • the present invention is particularly useful for preparing yeast-raised dough, baked or par-baked products in industrialized processes in which the dough used to prepare the baked or par-baked products are prepared mechanically using automated or semi-automated equipment.
  • the process of preparing bread generally involves the sequential steps of dough making (with an optional proofing step), sheeting or dividing, shaping or rolling, and proofing, the dough, which steps are well known in the art. If the optional proofing step is used, preferably more flour is added and alkali may be added to neutralize acid produced or to be produced during the second proofing step. In an industrial baked production process according to the present invention, one or more of these steps is/are performed using automated or semi-automated equipment, such as:
  • Horizontal mixers Roller bar mixers equipped with rotating arms, which in old models have two speed settings, typically, slow mixing at 35 rpm and fast mixing at 70 rpm, while newer models more often have variable speed settings ranging from 15-120 rpm.
  • Spiral mixers are typically mixers with a rotating bowl and a spiral counteracting the rotation. Some spiral mixers can be bidirectional to provide better distribution of the ingredients.
  • the purpose of mixing is uniform blending and hydration of dry material, kneading of the dough to form a gluten network and incorporation of air into the dough.
  • Two-speed mixing is usually employed with both types of mixers: A slow speed to collect the dough without pushing the dough to the side of the bowl, and a fast speed to assist formation of the gluten network.
  • the dough is mixed: a) at least 5 minutes at a slow mixing speed, preferably in the range of 5-50 rpm, more preferably in the range of 10-40 rpm; more preferably at least 10 minutes at a slow mixing speed, even more preferably at least 15 minutes a slow mixing speed; and optionally b) the dough is subsequently mixed at a faster speed.
  • the raw dough is baked normally, but halted at about approximately 80% of the normal cooking time, where after it is rapidly cooled.
  • a par-baked dough product bread can be transported easily, and stored until needed. Par-baked dough products are kept in sealed containers that prevent moisture loss. They are may be stored at room temperature; or stored in a fridge, or stored in a freezer.
  • the freezing step may lead to ice crystal formation and subsequent damage to the starch granules and amylose leakage. It is therefore likely that the amount of leaked amylose and unbound water is higher prior to the second bake-off than in a bread baked without a freezing step. These are two parameters known to increase the crumb firming rate.
  • a par-baked product is “finished off” by baking it at normal temperatures for an additional time, typically 5 to 15 minutes. The exact time must be determined by testing, as the time varies depending on the product.
  • the product may be stored at ambient/room temperature, or the product may be stored a low temperature, which means that it will normally be stored at a temperature below 5 degrees Celsius. In one embodiment, the product will be stored in a freezer.
  • Examples are bread (in particular white, whole-meal or rye bread), typically in the form of loaves or rolls, bread, flat bread, pita bread, tortillas, cakes, pancakes, biscuits, wafers, cookies, pie crusts, pizza, and the like.
  • Glucoamylases are also called amyloglucosidases, and Glucan 1 ,4-alpha-glucosidase (EC 3.2.1.3), more commonly they are referred to as AMGs.
  • amyloglucosidases may be used as parent for the generation of a thermostable amyloglucosidase variant, e.g, the amyloglucosidase may be a polypeptide that is encoded by a DNA sequence that is found in a fungal strain of Aspergillus, Rhizopusor, Talaromyces (Rasamsonia) or Penicilliurrr, preferably the DNA sequence that is found in a fungal strain of Penicillium, even more preferably the DNA sequence that is found in a fungal strain of Penicillium oxysporum, Penicillium oxalicum, Penicillium miczynskii, Penicillium russellii or Penicillium glabrum.
  • the parent glucoamylase is from a species of Penicillium, preferably from Penicillium oxicalum, Penicillium miczynskii, Penicillium russellii
  • thermostable glucoamylase variant of the invention comprises one or more or all of the combinations of amino acid substitutions listed in table 2 below.
  • the mature variant of the invention comprises at least one amino acid modification in one or more or all of the positions corresponding to positions 1 , 2, 4, 6, 7, 11, 31 , 34, 50, 65, 79, 103, 132, 327, 445, 447, 481, 484, 501 , 539, 566, 568, 594 and 595 in SEQ ID NO:1; preferably the at least one amino acid modification comprises a substitution in one or more or all of the positions corresponding to positions 1 , 2, 4, 11, 65, 79 and 327 in SEQ ID NO:1, preferably the at least one amino acid modification comprises a substitution in one or more or all of the positions corresponding to R1A, P2N, P4S, P11 F, T65A, K79V and Q327F in SEQ ID NO:1; or preferably the at least one amino acid modification comprises a substitution in one or more or all of the positions corresponding to positions 1, 6, 7, 31 , 34, 79, 103, 132, 445, 447, 48
  • thermostability improvements (Td) of the variants in table 2 are listed in Table 3, where the Td of the PoAMG variant denoted “anPAV498” (the parent) was set to zero.
  • the the mature thermostable variant of the invention has a thermostability improvement (Td) over its parent of at least 5°C, preferably at least 6°C, 7°C or 8°C, preferably determined as exemplified herein.
  • the mature thermostable variant of the invention has a relative activity at 91 °C of at least 150, preferably at least 200, more preferably at least 250, most preferably at least 300 compared to its parent.
  • the phospholipase enzymes may be prokaryotic, particularly bacterial, or eukaryotic, e.g., from fungal or animal sources.
  • Phospholipase enzymes may be derived, e.g., from the following genera or species: Thermomyces, T. lanuginosus (also known as Humicola lanuginosa); Humicola, H. insolens; Fusarium, F. oxysporum, F. solani, F. heterosporum; Aspergillus, A. tubigensis, A. niger, A. oryzae; Rhizomucor; Candida, C. antarctica, C. rugosa, Penicillium, P. camembertii; Rhizopus, Rhizopus oryzae; Absidia, Dictyostelium, Mucor, Neurospora, Rhizopus, R.
  • the phospholipase enzyme may be produced in a suitable host cell as known in the art.
  • Phospholipase may also be obtained from bee or snake venom or from mammal pancreas, e.g., porcine pancreas.
  • WO 98/26057 discloses a lipase/phospholipase from Fusarium oxysporum and its use in baking.
  • WO 2004/099400 discloses various phospholipase enzymes and their use in baking for reduction of dough stickiness.
  • Suitable commercial phospholipase preparations are Lipopan FTM, Lipopan XtraTM, and Lipopan PrimeTM (available from Novozymes A/S).
  • PanamoreTM available from DSM.
  • Lipopan FTM and Lipopan 50 BGTM available from Novozymes A/S.
  • Alpha-Amylases (alpha-1, 4-glucan-4-glucanohydrolases, EC. 3.2.1.1) constitute a group of enzymes which catalyze hydrolysis of starch and other linear and branched 1 ,4-glucosidic oligo- and polysaccharides.
  • alpha-amylases are referred to as TermamylTM, Termamyl® SC and “TermamylTM- like alpha-amylases” and are known from, e.g., WO 90/11352, WO 95/10603, WO 95/26397, WO 96/23873 and WO 96/23874.
  • alpha-amylases are referred to as FungamylTM and “FungamylTM-like alphaamylases”, which are alpha-amylases related to the alpha-amylase derived from Aspergillus oryzae disclosed in WO 01/34784.
  • a preferred group of alpha-amylases are referred to as maltogenic alpha-amylases (EC 3.2.1.133), typically derived from Bacillus stearothermophilus.
  • Preferred maltogenic alpha-amylases have an amino acid sequence at least 70% identical to SEQ ID NO:11 herein, e.g. at least 71 %, e.g. at least 72%, e.g. at least 73%, e.g. at least 74%, e.g. at least 75%, e.g. at least 76%, e.g. at least 77%, e.g. at least 78%, e.g. at least 79%, e.g., at least 80%, e.g.
  • sugar-tolerant maltogenic alpha-amylase variants such as the ones disclosed in WO 2006/032281 (Novozymes A/S), where a number of sugar-tolerant variants are provided, the variants each comprise an amino acid alteration which is a substitution or deletion of or insertion adjacent to 115, R18, K44, N86, T87, G88, Y89, H90, Y92, W93, F188, T189, 0190, P191 , A 192, F194, L196, 0329, N371 , 0372, P373, N375 or R376.
  • ST-MAA1 sugar-tolerant maltogenic alpha-amylase 1
  • ST-MAA2 sugar-tolerant maltogenic alpha-amylase 1
  • ST- MAA2 sugar-tolerant maltogenic alpha-amylase 2
  • ST- MAA2 sugar-tolerant maltogenic alpha-amylase 2
  • WO 2004/111217 discloses a number of preferred non-maltogenic thermostable variants of a Pseudomonas saccharophilia exoamylase or maltotetrahydrolase having the amino acid sequence shown in SEQ ID NO:12, the variants each comprise one or more of the following substitutions: G69P, A141 P, G223A, A268P, G313P, S399P and G400P.
  • WO 2007/148224 discloses more preferred mature non-maltogenic antistaling variants of a Pseudomonas saccharophilia exoamylase having the amino acid sequence shown in SEQ ID NO: 12, the variants each comprise an amino acid substitution at position 307 to lysine (K) or arginine (R).
  • WO 2010/133644 discloses other preferred mature non-maltogenic variants of a Pseudomonas saccharophilia exoamylase having the amino acid sequence shown in SEQ ID NO: 12, the variants each comprise one or more substitutions in positions including position 42, 88, 205, 223, 235, 240, 311 , 392, and 409.
  • One such preferred variant of the Pseudomonas saccharophilia exoamylase is disclosed in SEQ ID NO:31 of WO 2010/133644, its amino acid sequence is also shown in SEQ ID NO:13 herein and we denote it: HPL G+.
  • Pseudomonas saccharophilia exoamylase is disclosed in SEQ ID NO:21 of WO 2007/148224, its amino acid sequence is also shown in SEQ ID NO:14 herein and we denote it: HPL G4.
  • a preferred mature non-maltogenic alpha-amylase has an amino acid sequence at least 70% identical to SEQ ID NO:12, 13 or 14 herein, e.g. at least 71%, e.g. at least 72%, e.g. at least 73%, e.g. at least 74%, e.g. at least 75%, e.g. at least 76%, e.g. at least 77%, e.g. at least 78%, e.g. at least 79%, e.g., at least 80%, e.g. at least 81%, e.g. at least 82%, e.g. at least 83%, e.g.
  • At least 84% e.g., at least 85%, e.g. at least 86%, e.g. at least 87%, e.g. at least 88%, e.g. at least 89%, e.g., at least 90%, e.g., at least 91%, e.g., at least 92%, e.g., at least 93%, e.g., at least 94%, e.g., at least 95%, e.g.
  • the preferred mature non-maltogenic alpha-amylase has one or more of the substitutions listed in the above paragraph.
  • the raw starch degrading alpha-amylase is a GH13_1 amylase.
  • the raw starch degrading alpha-amylase enzyme has an amino acid sequence at least 70%, e.g. at least 71%, e.g. at least 72%, e.g. at least 73%, e.g. at least 74%, e.g. at least 75%, e.g. at least 76%, e.g. at least 77%, e.g. at least 78%, e.g. at least 79%, e.g., at least 80%, e.g. at least 81%, e.g. at least 82%, e.g. at least 83%, e.g. at least 84%, e.g., at least 85%, e.g.
  • one or more additional enzyme is added to the dough, said additional enzyme may be selected from the group consisting of a alpha amylase, maltogenic amylase, raw-starch degrading alpha amylase, beta amylase, aminopeptidase, carboxypeptidase, catalase, cellulase, chitinase, cutinase, cyclodextrin glycosyltransferase, deoxyribonuclease, esterase, glucan 1 ,4-alpha-maltotetrahydrolase, glucanase, beta glucanase, galactanase, alpha-galactosidase, beta-galactosidase, glucose oxidase, alpha-glucosidase, beta-glucosidase, haloperoxidase, hemicellulytic enzyme, invertase, laccase, lipase, mann
  • thermostable variant glucoamylase of the invention as well as any additional enzyme(s) may be added in any suitable form, such as, e.g., in the form of a liquid, in particular a stabilized liquid, or it may be added as a substantially dry powder or granulate.
  • Granulates may be produced, e.g., as disclosed in US Patent No. 4,106,991 and US Patent No. 4,661 ,452.
  • Liquid enzyme preparations may, for instance, be stabilized by adding a sugar or sugar alcohol or lactic acid according to established procedures. Other enzyme stabilizers are well-known in the art.
  • the enzyme(s) may be added in any suitable manner, such as individual components (separate or sequential addition of the enzymes) or addition of the enzymes together in one step or one composition.
  • Granulates and agglomerated powders may be prepared by conventional methods, e.g., by spraying the enzymes onto a carrier in a fluid-bed granulator.
  • the carrier may consist of particulate cores having a suitable particle size.
  • the carrier may be soluble or insoluble, e.g. a salt (such as NaCI or sodium sulfate), a sugar (such as sucrose or lactose), a sugar alcohol (such as sorbitol), starch, rice, corn grits, or soy.
  • a forward or reverse primer having NNK or desired mutation(s) at target site(s) with 15 bp overlaps each other were designed.
  • Inverse PCR which means amplification of entire plasmid DNA sequences by inversely directed primers, were carried out with appropriate template plasmid DNA (e.g. plasmid DNA containing JPG-0001 gene) by the following conditions.
  • the resultant PCR fragments were purified by QIAquick Gel extraction kit [QIAGEN], and then introduced into Escherichia coli ECOS Competent E.coli DH5a [NIPPON GENE CO., LTD.].
  • the plasmid DNAs were extracted from E. coli transformants by Mag Extractor plasmid extraction kit [TOYOBO], and then introduced into A. niger competent cells.
  • B. subtilis libraries constructed as in EXAMPLE 1 were fermented in either 96-well or 24- well MTP containing COVE liquid medium (2.0 g/L sucrose, 2.0 g/L iso-maltose, 2.0 g/L maltose, 4.9 mg/L, 0.2ml/L 5N NaOH, 10ml/L COVE salt, 10ml/L 1M acetamide), 32°C for 3days. Then, AMG activities in culture supernatants were measured at several temperatures by pNPG assay described as follows. pNPG thermostability assay:
  • the culture supernatants containing desired enzymes was mixed with same volume of pH 5.0 200 mM NaOAc buffer. Twenty microliter of this mixture was dispensed into either 96-well plate or 8-strip PCR tube, and then heated by thermal cycler at various temperatures for 30 min. Those samples were mixed with 10 pl of substrate solution containing 0.1% (w/v) pNPG [wako] in pH 5.0 200 mM NaOAc buffer and incubated at 70°C for 20 min for enzymatic reaction. After the reaction, 60 pl of 0.1 M Borax buffer was added to stop the reaction. Eighty microliter of reaction supernatant was taken out and its OD405 value was read by photometer to evaluate the enzyme activity.
  • Table 1a Lists of the relative activity of PoAMG variants when compared with their parent anPAV498 or JPO-0001 (anPAV498 w. Ieader-/propeptide)
  • Table 1b Lists of the relative activity of PoAMG variants when compared with their parent JPO- 022
  • Table 1c Lists of the relative activity of PoAMG variants when compared with their parent JPO- 063 at different temperatures
  • Table 1d List of the relative activity of PoAMG variants when compared with their parent JPO-
  • Table 1e List of the relative activity of PoAMG variants when compared with their parents JPO- 129
  • Aspergillus niger strains were fermented on a rotary shaking table in 500 ml baffled flasks containing 100ml MU1 with 4ml 50% urea at 220 rpm, 30°C.
  • the culture broth was centrifuged (10,000 x g, 20 min) and the supernatant was carefully decanted from the precipitates.
  • PoAMG variants were purified by cation exchange chromatography. The peak fractions of each were pooled individually and dialyzed against 20 mM sodium acetate buffer pH 5.0, and then the samples were concentrated using a centrifugal filter unit (Vivaspin Turbo 15, Sartorius). Enzyme concentrations were determined by A280 value.
  • Purified enzyme was diluted with 50 mM sodium acetate buffer pH 5.0 to 0.5 mg/ml and mixed with equal volume of SYPRO Orange (Invitrogen) diluted with Milli-Q water. Eighteen ul of mixture solution were transfer to LightCycler 480 Multiwell Plate 384 (Roche Diagnostics) and the plate was sealed.
  • the obtained fluorescence signal was normalized into a range of 0 and 1.
  • the Td was defined as the temperature at which the signal intensity was 0.5.
  • the thermostability improvements are listed in Table 3 with Td of the PoAMG variant denoted anPAV498 as 0.
  • Breads were baked in a straight dough baking process with a recipe according to Table 4. Different treatments were made according to Table 5 The bread was baked in open pans. The ingredients were mixed in a spiral mixer into a dough for 3 min at 17 rpm and 7 min at 35 rpm. The doughs were allowed to rest for 10 minutes and divided into 320 g dough pieces. The dough pieces were rounded sheeted and place in baking tins. The tins with the doughs were proofed for 60 min at 32°C and 86% relative humidity. The proofed doughs were baked in a deck oven for 20 min at 180 °C.
  • the texture of the bread was evaluated with a texture analyzer (TA-XT plus, Stable microsystems, Godalmine, UK).
  • Bread crumb texture properties were characterized by firmness (the same as “hardness” and the opposite of “softness”) and the elasticity of the baked product.
  • a standard method for measuring firmness and elasticity is based on force-deformation of the baked product.
  • a force-deformation of the baked products may be performed with a 40 mm diameter cylindrical probe. The force on the cylindrical probe is recorded as it is pressed down 40% strain on a 25 mm thick bread slice at a deformation speed of 1 mm/second. The probe is then kept in this position for 30 seconds while the force is recorded and then probe returns to its original position.
  • Firmness in grams is defined as the force needed to compress a probe to a 25% strain (corresponding to 6.25 mm compression into a bread crumb slice of 25 mm thickness).
  • Table 6 Firmness of bread crumb at different timepoints. The letter behind the number represents significance levels using a student t-test with a significance level of 0.05.
  • Table 7 Elasticity of bread crumb at different timepoints.
  • the letter behind the number represents significance levels using a student t-test with a significance level of 0.05.

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Abstract

L'invention concerne des procédés de production d'un produit cuit ou partiellement cuit comprenant la fourniture d'une pâte comprenant une protéine de légumineuse ajoutée et un variant thermostable mature d'une glucoamylase parente au moins 70 % identique à SEQ ID NO : 1, SEQ ID NO : 6, SEQ ID NO : 7, SEQ ID NO : 8 ou SEQ ID NO : 10; et la cuisson ou la cuisson partielle de la pâte pour produire le produit cuit ou partiellement cuit.
EP22829700.8A 2022-10-24 2022-11-30 Procédé de cuisson pour pain enrichi en protéine pulsée utilisant de l'amyloglucosidase thermostable (ec 3.2.1.3) Pending EP4608148A1 (fr)

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