WO2013092731A1 - Procédé de fabrication d'une pâte avec une glutamyl-endopeptidase - Google Patents

Procédé de fabrication d'une pâte avec une glutamyl-endopeptidase Download PDF

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Publication number
WO2013092731A1
WO2013092731A1 PCT/EP2012/076178 EP2012076178W WO2013092731A1 WO 2013092731 A1 WO2013092731 A1 WO 2013092731A1 EP 2012076178 W EP2012076178 W EP 2012076178W WO 2013092731 A1 WO2013092731 A1 WO 2013092731A1
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Prior art keywords
dough
protease
glutamyl
mix
products
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PCT/EP2012/076178
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English (en)
Inventor
Neil Carr
José MASTENBROEK
Luppo Edens
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Dsm Ip Assets B.V.
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Publication of WO2013092731A1 publication Critical patent/WO2013092731A1/fr

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    • A—HUMAN NECESSITIES
    • A21—BAKING; EDIBLE DOUGHS
    • A21D—TREATMENT, e.g. PRESERVATION, OF FLOUR OR DOUGH, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS; PRESERVATION THEREOF
    • 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, e.g. PRESERVATION, OF FLOUR OR DOUGH, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS; PRESERVATION THEREOF
    • 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
    • A21D2/265—Vegetable proteins from cereals, flour, bran

Definitions

  • the present invention relates to a method for preparing a dough.
  • a method for preparing a dough by using proteases in particular glutamyl specific proteases.
  • dough relaxants It is common to use dough relaxants in the baking industry.
  • additives such as I- cysteine or yeast derivatives rich in glutathione find common use in order to increase the extensibility of the gluten proteins in the dough.
  • Such dough relaxants are especially useful for the manufacture of bread rolls, pizzas, and tortillas so that products can be formed optimally. Dough relaxation is also critical within wider bakery applications when these use flour sources that are overly strong in terms of the gluten protein.
  • SMS sodium metabisulfite
  • Sodium metabisulfite reduces the gluten protein to increase extensibility of the dough, such that the dough can be sheeted more satisfactorily without shrinkage.
  • a disadvantage of SMS is that it may be an allergen to certain people.
  • proteases are used as alternatives to SMS and other dough relaxants.
  • proteases can be used to assist in the breakdown of gluten in hard doughs.
  • Commonly used commercial endoproteases include papain, bacillolysin, and thermolysin, and subtilisin.
  • these commercial preparations are perceived as leading to excessive digestion of gluten, and are therefore not favoured by, for example, the biscuit industry.
  • the main drawback is that their action is progressive. In other words, the breakdown continues while the dough stands. If this breakdown is achieved by mechanical or chemical means, there is no further reaction after the required degree is obtained.
  • the amount of gluten softening produced by a reductant, such as SMS, is dependent only on the amount added, while enzyme effects depend both on the amount added, temperature and the length of time allowed for protease action. Progressive digestion is perceived as problematic, especially if reworked dough is used, since dough characteristics may change with different standing times, which influences the quality and commercial value of the end product.
  • Figure 1 Proteolytic specificity of protease derived from Bacillus as determined upon incubation with ZAAX-pNA with Xaa representing the amino acid residue (in the one-letter code) preceding pNA.
  • Figure 2 Proteolytic specificity of protease derived from Staphylococcus as determined upon incubation with ZAAX-pNA with Xaa representing the amino acid residue (in the one- letter code) preceding pNA.
  • the present invention relates to a method for relaxing dough in the process of making a bakery product
  • the method comprises using a protease which has high specificity for glutamyl residues as the only proteolytic component in the dough and as a dough relaxant.
  • One advantage of the method according to the invention is that the method according to the invention allows for improved doughs. Without wishing to be bound by any theory, the inventor(s) believe that using the method according to the invention improved doughs are obtained because excessive digestion of the gluten in the dough is prevented and a more controlled breakdown of gluten is achieved.
  • the improved doughs have improved texture and structure compared to a reference dough in which no protease was used which has high specificity for glutamyl residues as the only proteolytic component and as a dough relaxant. This is in particular of importance when a reworked dough, viz. a dough that has been mixed and processed and added back to a fresh batch of dough, is involved.
  • a protease which has high specificity for glutamyl residues is also referred to as a glutamate-specific protease, glutamyl endoprotease or glutamic acid specific protease.
  • the term 'protease' is interchangeably used with the term 'endoprotease' and the term 'endopeptidase' and refers to an enzyme which catalyzes the cleavage of peptide bonds in other proteins or polypeptides, wherein the peptide bonds are distinct from the amino or carboxy termini of the substrate protein or polypeptide. It may belong to any of the groups into which endoproteases are commonly classified, viz. serine proteases, aspartic proteases, cysteine proteases and metalloproteases, which refer to their catalytic mechanism.
  • the protease which is used in the method according to the invention may be any type of protease, be it a neutral protease, an acidic protease or an alkaline protease.
  • it is an alkaline protease, which refers to a protease which has its pH optimum between about pH 8 and 12.
  • the protease which is used in the method according to the invention may be obtainable from any organism, be it a plant, animal or microorganism, such as a bacterium, fungus, yeast or virus. In one embodiment it is obtainable from a prokaryotic cell, e.g. a Gram-negative or Gram-positive bacterium.
  • Suitable bacteria include Escherichia, Anabaena, Caulobactert, Gluconobacter, Rhodobacter, Pseudomonas, Paracoccus, Bacillus, Brevibacterium, Corynebacterium, Rhizobium (Sinorhizobium), Flavobacterium, Klebsiella, Enterobacter, Lactobacillus, Lactococcus, Methylobacterium, Moraxella, Neisseria, Staphylococcus, Streptomyces or Thermoactinomyces.
  • a bacterial cell in particular from a Staphylococcus, Streptomyces, Thermoactinomyces or a Bacillus, more in particular from an S. aureus, B. subtilis, B. amyloliquefaciens, B. licheniformis, B. intermedius, B. puntis, B. megaterium, B. halodurans or B. pumilus.
  • the protease is obtainable from a eukaryotic cell.
  • the eukaryotic cell is a mammalian, insect, plant, fungal, or algal cell.
  • Preferred mammalian cells include e.g. Chinese hamster ovary (CHO) cells, COS cells, 293 cells, PerC6 cells, and hybridomas.
  • Preferred insect cells include e.g. Sf9 and Sf21 cells and derivatives thereof.
  • the eukaryotic cell is a fungal cell, i.e. a yeast cell, such as Candida, Hansenula, Kluyveromyces, Pichia, Saccharomyces, Schizosaccharomyces, or Yarrowia strain.
  • the eukaryotic cell is a filamentous fungal cell.
  • Filamentous fungi include all filamentous forms of the subdivision Eumycota and Oomycota (as defined by Hawksworth et al , In, Ainsworth and Bisby's Dictionary of The Fungi, 8th edition, 1995, CAB International, University Press, Cambridge, UK).
  • Filamentous fungal strains include strains of Acremonium, Agaricus, Aspergillus, Aureobasidium, Chrysosporium, Coprinus, Cryptococcus, Filibasidium, Fusarium, Humicola, Magnaporthe, Mucor, Myceliophthora, Neocallimastix, Neurospora, Paecilomyces, Penicillium, Piromyces, Panerochaete, Pleurotus, Schizophyllum, Talaromyces, Thermoascus, Thielavia, Tolypocladium, and Trichoderma.
  • Preferred filamentous fungal cells belong to a species of an Aspergillus, Chrysosporium, Penicillium, Talaromyces, Fusarium or Trichoderma genus, and most preferably a species of Aspergillus niger, Aspergillus awamori, Aspergillus foetidus, Aspergillus sojae, Aspergillus fumigatus, Talaromyces emersonii, Aspergillus oryzae, Chrysosporium lucknowense, Myceliophtora thermophila, Fusarium oxysporum, Trichoderma reesei or Penicillium chrysogenum.
  • the protease may be obtained by any means available in the art, including genetic engineering techniques, such as cloning, mutation and nucleotide or protein synthesis.
  • the protease may be comprised in a preparation comprising or consisting of the protease.
  • the protease preparation may comprise between 0.001 % and 100% w/w of the protease based on total protein.
  • the preparation comprises between 1 % and 70% w/w of the protease based on total protein.
  • the preparation comprises between 1 % and 50% w/w of the protease based on total protein.
  • the preparation comprises between 1 % and 30% w/w of the protease based on total protein.
  • the protease may be the major enzymatic component in the preparation.
  • the protease preparation may comprise several enzymatic activities, as long as they do not interfere with the benefits offered by the method according to the invention. This means that excessive relaxation of the dough, most likely due to excessive digestion of the gluten, must be prevented. Therefore, the protease is preferably the only proteolytic component, in any case the only functioning proteolytic component, present in the preparation.
  • the protease which is used in the method according to the invention has high specificity towards glutamyl residues in a polypeptide chain.
  • an enzyme is said to have 'specificity' for a certain amino acid when under given circumstances the peptide bond at the carboxy or amino terminal site of the certain amino acid is cleaved with a preference substantially in excess of other peptide bonds.
  • 'high specificity' refers to a preference for cleavage at a peptide bond of a certain amino acid, whereby the preference is in excess at least three fold , preferably at least four fold , preferably at least five fold , preferably at least six fold relative to any other peptide bond.
  • Glutamyl endopeptidases (EC 3.4.21.19) have high specificity for cleaving at the carboxy terminal side of glutamyl residues.
  • Suitable glutamyl endopeptidases which may be used in the method according to the present invention are glutamyl endopeptidases which cleave at the glutamyl residue with a preference in excess of at least five fold, preferably at least six fold, at least seven fold, at least eight fold, at least nine fold, at least ten fold, relative to any other amino acids.
  • Some endoprotease have broad specificity and hydrolyse peptide bonds of, for example, (all) hydrophobic residues. Although they may have certain specificity for glutamyl residues, they will not have high specificity for glutamyl residues, and therefore such proteases should not be used in the method according to the invention, because this may lead to excessive relaxation of the dough, most likely due to excessive digestion of the gluten. On the other hand, if a protease has high specificity for glutamyl residues, and (low) specificity for peptide bonds adjacent to other amino acids residues, it may still be used in the method according to the invention as long as it does not lead to excessive relaxation of the dough, most likely due to excessive digestion of the gluten.
  • One unit (U) of the glutamyl endopeptidolytic activity is defined as the amount of enzyme required for the production of 1 ⁇ p-nitroanilide per minute
  • the method comprises contacting the dough with a protease which has a high specificity for glutamyl residues, wherein said high specificity is defined as a preference for a glutamyl peptide bond of at least three fold, preferably at least four fold, preferably at least five fold, preferably at least six fold, preferably at least seven fold, preferably at least eight fold, relative to a peptide bond of any other amino acid residue as determined via incubating 1 ,25 mM (millimol/l) solutions of ZAAX-p-nitroanilide comprising 10 microgram/ml, preferably purified, protease in a buffer containing 100 mM MES buffer of pH 6.5 at 37°C for a period of 30 min and after these 30 minutes measuring the optical density at 405 nm, using 1 ,25 mM (millimol/l) solutions of ZAAX-p-nitroanilide in the buffer containing 100 mM MES buffer of pH 6.5
  • X represents either A, I, L, V, S, G, P, Q, E, R, D, K, N, Y, H or F.
  • the one-letter code of amino acids used herein is commonly known in the art and can be found in Sambrook, et al. (Molecular Cloning: A Laboratory Manual, 2nd,ed. Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1989).
  • A stands for Alanine, I for Isoleucine, L for Leucine, V for Valine, S for Serine, G for Glycine, P for Proline, Q for Glutamine, E for Glutamic acid, R for Arginine , D for Aspartic acid , K for Lysine, N for Asparagine, Y for Tyrosine, H for Histidine , F for Phenylalanine ⁇ for Cysteine, T for Threonine.
  • Dough relaxation refers to reduced elasticity within the dough. Dough relaxation can be measured by a number of established techniques that characterise the rheology of dough, for example by oscillatory rheometry, or by stress-relaxation tests (see Zaidel et al, J. Applied Sciences 10:2478-2480, 2010) or, more satisfactorily, through the evaluation of the dough during processing such that the dough exhibits a reduced tendency to contract after lamination and an increased tendency for extensional flow during handling and proof.
  • the term 'gluten' refers to the protein composite found in wheat and related grains, such as rye and barley. Gluten is an important constituent of the flour used for making doughs and gives cohesiveness to dough.
  • the gluten may be any gluten, be it from wheat, rye or barley.
  • the gluten is wheat gluten.
  • Wheat gluten is formed from the proteins gliadin and glutenin.
  • the term 'dough' refers to an elastic, pliable protein network mixture that minimally comprises a flour, or meal and a liquid, such as milk or water, which is typically used to prepare a food product.
  • a typical dough may comprise, in addition to the flour, or meal and the liquid, such as milk or water, one or more of the following ingredients: grain, yeast, sponge, salt, shortening, sugar, yeast nutrients, dough conditioners and preservatives.
  • the dough may be any dough, in particular a dough for baked goods.
  • the term 'baked good' refers to baked or to be baked food products, including bread (e.g. rye, wheat, oat, potato, white, whole grain products, mixed flours, loaves, twists, buns, rolls, pitas, matzos, focaccia, melba toast, zwieback, croutons, soft pretzels, soft and hard bread, bread sticks), such as yeast leavened and chemically-leavened bread, white bread, variety breads, rolls, muffins, cakes, danish, croissants, bagels, cookies, in particular biscuits, confectionery coatings, crackers, doughnuts and other sweet pastry goods, pie and pizza crusts, pretzels, pita and other flat breads, tortillas, pasta products, par-baked products and refrigerated and frozen dough products.
  • bread e.g. rye, wheat, oat, potato, white, whole grain products, mixed flours, loaves, twists, buns, rolls, pitas, matzo
  • the dough and the glutamyl endoprotease may be brought into contact by any suitable way. Typically, this is done by adding the glutamyl endoprotease to the flour which is used to prepare the dough.
  • the dough comprising the glutamyl endoprotease may be kneaded and rested for at least 5 min, at least 10 min, at least 30 min, at least 45 min, at least 60 min, at least 75 min, at least 90 min, at least 120 min, without negative effects to the characteristics of the dough or of the end product.
  • the protease may be added before kneading or during kneading. The method of the invention is particularly advantageous for doughs which are reworked.
  • the amount of glutamate specific protease to be added to the flour for the dough will vary depending on the type of flour used, the desired degree of digestion and the duration of the digestion.
  • the amount of peptidase added will typically range from about 1 unit of enzyme per kg flour to about 2000 units of enzyme per kilogram of flour.
  • 50 - 2000 units of enzyme per kg flour is used, more preferably, 100-1000 units of enzyme per kg flour is used.
  • the duration of the digestion will vary, depending on the circumstances and the application. Generally speaking, the duration of the digestion may range from a few minutes to many hours, such as, from about 5 or 10 minutes to about 1 hour or 2 hours.
  • the digestion will end when all the peptide substrates for the protease have been converted.
  • the peptidase may be inactivated actively, for example by heating the dough. In both cases, excessive relaxation of the dough, probably due to excessive digestion of the gluten, will be prevented.
  • the present invention relates to the use of a protease for the relaxation of a dough. All the embodiments which were mentioned above, with all the preferences mentioned above, also apply to this aspect of the invention.
  • the present invention relates to a dough obtained by a method according to the invention.
  • the dough may be used in baking, to prepare a baked or bakery product, such as a bread product (e.g. rye, wheat, oat, potato, white, whole grain products, mixed flours, loaves, twists, buns, rolls, pitas, matzos, focaccia, melba toast, zwieback, croutons, soft pretzels, soft and hard bread, bread sticks), such as yeast leavened and chemically-leavened bread, white bread, variety breads, rolls, muffins, cakes, danish, croissants, bagels, cookies, in particular biscuits, confectionery coatings, crackers, doughnuts and other sweet pastry goods, pie and pizza crusts, pretzels, pita and other flat breads, tortillas, pasta products, par-baked products and refrigerated and frozen dough products.
  • a bread product e.g. rye, wheat, oat, potato, white,
  • the dough is a biscuit dough.
  • Baked products obtained by using a dough prepared according to the method according to the invention are also encompassed by the present invention. All the embodiments which were mentioned above, with all the preferences mentioned above, also apply to doughs and baked products according to the invention.
  • the bacterial glutamyl endopeptidases (EC 3.4.21 .19) may be divided into three groups according to the source organisms and sequence relationships: a Staphylococcal group, a Bacillus group and a Streptomyces group (Handbook of Proteolytic Enzymes, A.J. Barrett, N.D. Rawlings and J.F. Woessner eds, Academic Press).
  • cleavage preferences of the glutamyl endopeptidases are exemplified by enzyme samples obtained from either Staphylococcus aureus (Sigma) or from Bacillus (over expressed and isolated essentially as described by Matsumoto et al.(J. Ferment. Bioeng.1995, 79,23-27)).
  • Results are shown in Figures 1 and 2.
  • the enzyme preparations in both cases were shown to have high specificity towards peptide cleavage at the glutamate residue, with a preference substantially in excess of ten-fold relative to the other amino acid residues.
  • Example 3 Comparison of dough rheology made with different formulations
  • One formulation contained sodium metabisulfite (SMS); another contained, glutamyl endopeptidase isolated from Staphylococcus aureus; and a formulation with a commercial bacillolysin (Bakezyme® Protease GBW from DSM, The Netherlands) with broad specificity, viz. which specificity for peptide bonds involving hydrophobic residues, such as leucine, isoleucine, phenylalanine and valine.
  • SMS sodium metabisulfite
  • glutamyl endopeptidase isolated from Staphylococcus aureus a formulation with a commercial bacillolysin (Bakezyme® Protease GBW from DSM, The Netherlands) with broad specificity, viz. which specificity for peptide bonds involving hydrophobic residues, such as leucine, isoleucine, phenylalanine and valine.
  • Doughs were prepared according to the formulation of Table 2a/b, using a Farinograph mixing bowl set at 40°C, and mixing 12 minutes beyond peak torque. Dough pieces were then held at 40°C allowing periodic rheological measurement to be made by means of a stress-relaxation test using a texture analyser fitted with a 45mm probe (Microstable TAXT2); the probe was compressed into a dough piece (15g) and compressed by 50% measuring the decay in force from its maximum value over a period of 25s. Results are provided in Table 3.
  • glutamyl endopeptidase brings substantial advantage over enzymes of broad cleavage specificity and forms an alternative to sodium metabisulfite.
  • Example 4 Semi-sweet biscuits made with formulations containing sodium metabisulfite and glutamyl endopeptidase isolated from Bacillus
  • the glutamyl endopeptidase brought closely similar influence to sodium metabisulfite on the properties of the dough and biscuits as can be seen by comparing the weights of the cut dough and those of the biscuits and, additionally, by the dimensions taken of the biscuits; secondly, and more importantly, the scale of influence remained of the same magnitude in spite of the enzyme being used over an 8 fold dose level.

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  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Food Science & Technology (AREA)
  • Microbiology (AREA)
  • Bakery Products And Manufacturing Methods Therefor (AREA)

Abstract

La présente invention concerne un procédé pour l'assouplissement d'une pâte dans le processus de fabrication d'un produit de boulangerie. Le procédé comprend l'utilisation d'une protéase qui a une haute spécificité pour résidus de glutamyle en tant qu'unique composant protéolytique dans la pâte pour accomplir l'assouplissement. Le procédé exclut la protéolyse étendue et la pâte peut être utilisée de manière satisfaisante industriellement pour préparer des produits de boulangerie, tels que du pain, des biscuits et des produits de pâte alimentaire. Le procédé est particulièrement adapté aux pâtes retravaillées.
PCT/EP2012/076178 2011-12-21 2012-12-19 Procédé de fabrication d'une pâte avec une glutamyl-endopeptidase WO2013092731A1 (fr)

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Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2018234382A1 (fr) * 2017-06-22 2018-12-27 Novozymes A/S Relaxation d'une pâte à l'aide d'une gamma glutamyle transpeptidase
WO2021023767A1 (fr) * 2019-08-07 2021-02-11 Novozymes A/S Procédé de relaxation de pâte impliquant des endopeptidases

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US4377602A (en) * 1977-10-18 1983-03-22 Nordstjernan Ab Process for the preparation of a hydrolyzed product from whole grain and such a product
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WO2003007731A1 (fr) * 2001-07-17 2003-01-30 Compagnie Laitiere Europeenne Lactoserum modifie, procede de preparation, utilisation et produit de panification comprenant le lactoserum modifie
WO2005077192A1 (fr) * 2004-02-17 2005-08-25 Wageningen Centre For Food Sciences Procede de preparation d'une pate a pain ou de pain precuit
WO2005117595A1 (fr) * 2004-06-04 2005-12-15 Dsm Ip Assets B.V. Methode d'amelioration du gout de produits a base de cereales cuits au four
US20070148302A1 (en) * 2005-12-27 2007-06-28 Ricardo Villota Nutritionally enhanced pasta

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MATSUMOTO ET AL., J. FERMENT. BIOENG., vol. 79, 1995, pages 23 - 27
SAMBROOK ET AL.: "Molecular Cloning: A Laboratory Manual", 1989, COLD SPRING HARBOR LABORATORY PRESS
ZAIDEL ET AL., J. APPLIED SCIENCES, vol. 10, 2010, pages 2478 - 2480

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2018234382A1 (fr) * 2017-06-22 2018-12-27 Novozymes A/S Relaxation d'une pâte à l'aide d'une gamma glutamyle transpeptidase
CN110719735A (zh) * 2017-06-22 2020-01-21 诺维信公司 使用γ谷氨酰基转肽酶松弛面团
WO2021023767A1 (fr) * 2019-08-07 2021-02-11 Novozymes A/S Procédé de relaxation de pâte impliquant des endopeptidases
CN114206117A (zh) * 2019-08-07 2022-03-18 诺维信公司 涉及内肽酶的面团松弛度的方法

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