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  • C12P19/00—Preparation of compounds containing saccharide radicals
  • C12P19/18—Preparation of compounds containing saccharide radicals produced by the action of a glycosyl transferase, e.g. alpha-, beta- or gamma-cyclodextrins
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23K—FODDER
  • A23K10/00—Animal feeding-stuffs
  • A23K10/10—Animal feeding-stuffs obtained by microbiological or biochemical processes
  • A23K10/14—Pretreatment of feeding-stuffs with enzymes
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23K—FODDER
  • A23K20/00—Accessory food factors for animal feeding-stuffs
  • A23K20/10—Organic substances
  • A23K20/163—Sugars; Polysaccharides
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
  • A23L29/30—Foods or foodstuffs containing additives; Preparation or treatment thereof containing carbohydrate syrups; containing sugars; containing sugar alcohols, e.g. xylitol; containing starch hydrolysates, e.g. dextrin
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
  • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
  • A23L33/125—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives containing carbohydrate syrups; containing sugars; containing sugar alcohols; containing starch hydrolysates
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
  • A23L33/20—Reducing nutritive value; Dietetic products with reduced nutritive value
  • A23L33/21—Addition of substantially indigestible substances, e.g. dietary fibres
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  • 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
  • C12N9/10—Transferases (2.)
  • C12N9/1048—Glycosyltransferases (2.4)
  • C12N9/1051—Hexosyltransferases (2.4.1)
• • 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
  • C12N9/10—Transferases (2.)
  • C12N9/1048—Glycosyltransferases (2.4)
  • C12N9/1051—Hexosyltransferases (2.4.1)
  • C12N9/107—1,4-Alpha-glucan branching enzyme (2.4.1.18)
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
  • C12P19/00—Preparation of compounds containing saccharide radicals
  • C12P19/04—Polysaccharides, i.e. compounds containing more than five saccharide radicals attached to each other by glycosidic bonds
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y204/00—Glycosyltransferases (2.4)
  • C12Y204/01—Hexosyltransferases (2.4.1)
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y204/00—Glycosyltransferases (2.4)
  • C12Y204/01—Hexosyltransferases (2.4.1)
  • C12Y204/01005—Dextransucrase (2.4.1.5)
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y204/00—Glycosyltransferases (2.4)
  • C12Y204/01—Hexosyltransferases (2.4.1)
  • C12Y204/01018—1,4-Alpha-glucan branching enzyme (2.4.1.18), i.e. glucan branching enzyme
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y204/00—Glycosyltransferases (2.4)
  • C12Y204/01—Hexosyltransferases (2.4.1)
  • C12Y204/01025—4-Alpha-glucanotransferase (2.4.1.25)
• • C—CHEMISTRY; METALLURGY
  • C13—SUGAR INDUSTRY
  • C13K—SACCHARIDES OBTAINED FROM NATURAL SOURCES OR BY HYDROLYSIS OF NATURALLY OCCURRING DISACCHARIDES, OLIGOSACCHARIDES OR POLYSACCHARIDES
  • C13K13/00—Sugars not otherwise provided for in this class

Definitions

• the present invention relates to a process for preparing a mixture of poorly digestible ⁇ -glucans from a substrate rich in oligosaccharides having a degree of polymerization (DP) of 4.
• this substrate means a syrup containing oligosaccharides with an oligosaccharide content having a degree of polymerization (DP) of 4 of at least 40%, preferably at least 45%, even more preferably at least 50%.
• the invention also relates to a mixture of poorly digestible a-glucans.
• the present invention also relates to the use of an a-glucanotransferase capable of creating a(1-6) glucosidic bonds to reduce the digestibility of a mixture of a-glucans.
• Dietary fibers have an important role in human nutrition. Among dietary fibers, we distinguish between soluble fibers, which are soluble in water and have a gelling capacity, and insoluble fibers. Soluble fibers, including branched maltodextrins, are particularly interesting because they are poorly digestible. As a result, their incorporation into the diet makes it possible to reduce the glycemic index of a food and prolong the feeling of satiety. They also have prebiotic properties on the intestinal flora, that is to say they are capable of selectively promoting the growth of certain probiotic type bacteria or the activity of the microbiota, providing a benefit to the health.
• alpha 1 —> 6 or alpha 1 —> 3 bonds By increasing the percentage of alpha 1 —> 6 or alpha 1 —> 3 bonds, the degree of branching of the maltodextrins is increased, which makes them more resistant to digestion.
• the Applicant company found that it was possible, from a syrup rich in oligosaccharides having a degree of polymerization (DP) of 4, to obtain fibers of interest in human and animal food, by enzymatic pathway.
• the Applicant company has thus developed a process which uses a particular enzyme, capable of creating a(1-6) bonds from syrup rich in DP4 oligosaccharides.
• the present invention relates to a process for preparing a mixture of a-glucans, preferably a mixture of branched maltodextrins, comprising a step of bringing a substrate and an enzyme, said substrate being a syrup rich in oligosaccharides having a degree of polymerization (DP) of 4 and said enzyme being an a-glucanotransferase capable of cleaving a(1-4) glucosidic bonds and creating a(1) glucosidic bonds -6).
• DP degree of polymerization
• a-glucan soluble fiber
• soluble dietary fiber oligosaccharides composed of at least 3 glucose units linked together by a-glycosidic (or a-glucosidic) bonds.
• a-glucans The classification of a-glucans is mainly based on the measurement of their reducing power, classically expressed by the notion of “dextrose equivalent” (“Dextrose Equivalent” or DE).
• DE Dextrose Equivalent
• maltodextrins included in the Monograph Specifications of the Food Chemical Codex specifies that the DE value for a maltodextrin must not exceed 20. Above 20, these are glucose syrups.
• Such a measurement of the DE is, however, insufficient to precisely represent the molecular distribution of ⁇ -glucans. Indeed, the acid hydrolysis of starch, completely random, or its enzymatic hydrolysis, a little more ordered, provide mixtures of glucose and glucose polymers that the sole measurement of the DE does not make it possible to define with precision, and which include molecules of short size, low DP, as well as molecules of very long size, DP. pupil.
• the measurement of the DE in fact only gives an approximate idea of the average DP of the mixture of glucose and the glucose polymers constituting the a-glucans and therefore of their number average molecular mass (Mn). To complete the characterization of the molecular mass distribution of a-glucans, the determination of another parameter is important, that of the weight average molecular mass (Mp).
• (Mn) and (Mp) are determined experimentally by different analysis techniques, such as for example a measurement method adapted to glucose polymers, which is based on gel permeation chromatography on columns. chromatography calibrated with pullulans of known molecular masses.
• the Mp/Mn ratio is called the polymolecularity index (PI) and makes it possible to globally characterize the distribution of molecular masses of a polymer mixture.
• PI polymolecularity index
• the process according to the present invention makes it possible to reduce the percentage of a(1-4) bonds in favor of a(1-6) bonds, which has the advantage of reducing the digestibility of the a-glucan mixture. obtained by the process.
• the mixture of ⁇ -glucans prepared according to the process of the invention is preferably a mixture of branched maltodextrins.
• branched maltodextrins means maltodextrins whose content of ⁇ (1-6) glucosidic bonds is greater than that of standard maltodextrins.
• Standard maltodextrins are defined as purified and concentrated mixtures of glucose and glucose polymers essentially linked in a(1-4) with only 4 to 5% of a(1-6) glucosidic bonds, molecular weight extremely varied, completely soluble in water and with low reducing power.
• the syrup rich in oligosaccharides having a DP of 4 comprises at least 40%, preferably at least 45%, even more preferably at least 50% of oligosaccharides having a DP of 4.
• the syrup rich in oligosaccharides having a DP of 4 has a dextrose equivalent (DE) greater than 20.
• the syrup rich in DP4 is a syrup having the characteristics described in Table 1 below.
• the substrate is present at a concentration of between 50 g/L and 500 g/L, preferably between 100 g/L and 200 g/L in the reaction medium.
• the ⁇ -glucanotransferase capable of cleaving ⁇ (1-4) glucosidic bonds and creating ⁇ (1-6) glucosidic bonds is the protein having the sequence SEQ ID No: 1 or a protein having at least 90% identity with the protein having the sequence SEQ ID No: 1 (hereinafter referred to as GT#19).
• it is a protein having at least 91%, even more preferably, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 96%.
• sequence SEQ ID No: 1 corresponds to the Genbank accession number WP_053069107.1.
• the inventors have shown that the GT#19 enzyme is capable of modifying a syrup rich in DP4 so as to make it poorly digestible, with a % hydrolysis according to the AQAC2002 method. 02 less than or equal to 45%).
• the enzyme is added at a concentration of between 0.01 and 1 mg/mL of reaction medium, preferably between 0.05 and 0.5 mg/mL, even more preferably approximately 0.1 mg/mL of reaction medium.
• the bringing together of the substrate and the enzyme is carried out for a period of between 12 and 48 hours, preferably approximately 24 hours.
• the bringing together of the substrate and the enzyme is carried out at a temperature between 20 and 40°C, preferably around 37°C.
• the bringing together of the substrate and the enzyme is carried out at a pH between 5 and 6.5, preferably between 5.5 and 6, even more so. preferred about 5.75.
• the method further comprises an enzymatic treatment step with an a-glucanotransferase capable of cleaving the a(1 -4) glucosidic bonds and creating a(1 -) glucosidic bonds.
• an a-glucanotransferase capable of cleaving the a(1 -4) glucosidic bonds and creating a(1 -) glucosidic bonds.
• It may for example be a protein having the sequence SEQ ID No:2 or a protein having at least 90% identity with the protein having the sequence SEQ ID No:2 (hereinafter referred to as GT#11) .
• GT#11 protein having at least 91%, even more preferably, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 96%.
• sequence SEQ ID No: 2 corresponds to the Genbank accession number AOR73699.1.
• the present invention also relates to a mixture of aglucans, preferably a mixture of branched maltodextrins, capable of being obtained by the process described above.
• This mixture of a-glucans is characterized by its low digestibility according to the AOAC 2002.02 method.
• the process according to the invention makes it possible to reduce by a factor of at least 2, preferably at least 2.5, even more preferably by at least 3, the hydrolyzable fraction, measured according to the AOAC 2002.02 method, compared to the starting substrate.
• the AOAC 2002.02 method can in particular be implemented using the “HPAEC-PAD assay” part of the “resistant Starch, K-RSTAR 06/18” kit marketed by the company Megazyme® as described in the Example 1, part 5 below.
• the method according to the present invention makes it possible to increase the percentage of ⁇ (1-6) bonds by a factor of at least 3, preferably at least 3.5, even more preferably at least 4. , relative to the starting substrate.
• the percentage of a(1 -6) bonds can be measured by the Hakomori method (1964 HAKOMORI A Rapid Permethylation of Glycolipid, and Polysaccharide Catalyzed by Methylsulfinyl Carbanion in Dimethyl Sulfoxide) as described in Example 1, part 8 below or by proton NMR as described in Example 1, part 7 below.
• the present invention relates to a mixture of a-glucans, preferably a mixture of branched maltodextrins, characterized in that it presents:
• a rate of hydrolyzable fibers less than 55%, preferably less than 50%, even more preferably less than 45%,
• a(1-6) bonds in which the fiber content corresponds to the hydrolyzable fraction (i.e. non-resistant) according to the AOAC 2002.02 method and the percentage of a bonds (1 -6) represents the molar percentage of a(1 -6) bonds relative to the total number of glycosidic bonds, measured by the Hakomori method.
• the rate of hydrolyzable fibers is less than 44%, preferably less than 43%, even more preferably less than 42%, 41%, 40%, 39%, 38%, 37%, 36%, 35%, 34%, 33%, 32%, 31%, 30%.
• the rate of hydrolyzable fibers is greater than 5%, preferably greater than 10%, 11%, 12%, 13%, 14%, 15%, 18%, 19%, 20%, 21 %, 22%, 23%, 24%, 25%.
• the rate of hydrolyzable fibers is between 5% and 45%, preferably between 10% and 45%, preferably between 20% and 44%, more preferably between 30% and 45%. % and 45%.
• the percentage of a(1-6) bonds is at least 21%, preferably at least 22%, even more preferably at least 23%, at least 24%, at least 25%, at least 26%, at least 27%, at least 28%, at least 29%, at least 30%, at least 31%, at least 32%, at least 33%, at least 34%, at least 35%.
• the percentage of a(1 -6) bonds is at most 40%, preferably at most 36%, at most 35%, at most 34%, d 'at most 33%, at most 32%, at most 31%.
• the percentage of a(1-6) bonds is between 20% and 40%, preferably between 20% and 35%, preferably between 25% and 35%.
• the percentage of a(1-3) bonds is at least 2%, preferably at least 3%.
• the percentage of a(1-3) bonds is at most 6%, preferably at most 5%.
• the percentage of ⁇ (1-3) bonds is between 2% and 8%, preferably between 3% and 5%.
• the percentage of a(1-2) bonds is at least 1%, preferably at least 2%.
• the percentage of a(1-2) bonds is at most 8%, preferably at most 6%, at most 5%, at most 4%. at most 3%.
• the percentage of a(1 -4) bonds is at most 80%, preferably at most 70%, at most 65%.
• the percentage of a(1 -4) bonds is at least 50%, preferably at least 55%, at least 60%.
• the percentage of ⁇ (1-4) bonds is between 50% and 80%, preferably between 55% and 70%, preferably between 55% and 65%.
• the mixture of ⁇ -glucans which is preferably a mixture of branched maltodextrins, is characterized in that it presents:
• a rate of hydrolyzable fibers less than 55%, preferably less than 50%, even more preferably less than 45%,
• a(1 -4) bonds in which the rate of fibers corresponds to the hydrolyzable fraction (i.e. non-resistant) according to the AOAC 2002.02 method and the percentage of a( 1-6), a(1 -3), a(1-2), or a(1 -4) represents the molar percentage of said type of bonds relative to the total number of glycosidic bonds, measured by the Hakomori method.
• said bond ratios a(1-6), a(1-3), a(1-2), or a(1-4) are such that the sum of their molar percentage is equal to 100%.
• the present invention also relates to the use of a mixture of ⁇ -glucans obtained according to the process described above and of a mixture of ⁇ -glucans having the properties described above for the preparation of food for human or animal consumption.
• the a-glucan mixture according to the invention can be used to promote intestinal health, blood sugar management, satiety and weight management, and sustained energy release.
• the present invention relates to the use of a glucanotransferase capable of cleaving ⁇ (1-4) glucosidic bonds and creating ⁇ (1-6) glucosidic bonds to reduce the digestibility of 'a mixture of ⁇ -glucans, said glucanotransferase having the sequence SEQ ID No: 1 or a protein having at least 90% identity with the protein having the sequence SEQ ID No: 1.
• the mixture of ⁇ -glucans is preferably a syrup rich in oligosaccharides, in particular a syrup rich in oligosaccharides having DP of 4 as described in the first aspect of the invention.
• the reduction in digestibility is a reduction by a factor of at least 2, preferably at least 2.5, even more preferably at least 3 of the hydrolyzable fraction, measured according to the AOAC 2002.02 method, relative to the starting substrate.
• the invention will be better understood with the aid of the examples which follow, which are intended to be illustrative and not limiting.
• Example 1 preparation of branched maltodextrins from syrup rich in DP4: materials and methods
• E. coli BL21 star cells containing the plasmid pET-21 a-enzyme no. % glycerol and 1% lactose.
• Cellular debris was separated from solubilized proteins by centrifugation for 30 min at 10,000 g.
• the determination of the different protein solutions was carried out by measuring their absorbance at 280 nm using a nanodrop 2000 spectrophotometer (Thermofisher). The molecular extinction coefficients were determined using the ProtParam tool application from the ExPASy bioinformatics resource portal site.
• the transfer reactions were lyophilized after freezing at -80° C. for 24 hours. 25 mg of lyophilized products were taken up in 1 mL of 100mM sodium maleate buffer containing 30 U of pancreatic a-amylase and 3 U of amyloglucosidase (Starch resistant kit, Megazyme K-STAR 06/18, which uses the AOAC 2002.02 method). The reactions were incubated for 16 hours at 37°C. The products were diluted in water before HPAEC PAD analysis.
• the products obtained were analyzed by anion exchange chromatography coupled with a pulsed amperometric detector (HPAEC PAD - High Performance Anion Exchange Chromatography with Pulsed Amperometric Detection).
• HPAEC PAD High Performance Anion Exchange Chromatography with Pulsed Amperometric Detection
• the analyzes were carried out on a Thermo ICS6000 system equipped with a CarboPacTM PA100 analytical column (2 mm x 250 mm) coupled with a CarboPacTM PA100 guard pre-column (2 mm x 50 mm).
• a gradient of sodium acetate in 150 mM sodium hydroxide was applied at a flow rate of 0.250 ml.min-1 according to the following profile: 0-5 min, 0 mM; 5-35 min, 0-300 mM; 35-40 min, 300-450 mM; 40-42 min, 450mM.
• Detection was carried out using a gold working electrode and an Ag/AgCI pH reference cell. The samples were diluted to a total dry mass of 1 g.L-1 before injection.
• the Hakomori method (1964 HAKOMORI A Rapid Permethylation of Glycolipid, and Polysaccharide Catalyzed by Methylsulfinyl Carbanion in Dimethyl Sulfoxide) makes it possible to chemically characterize the saccharide bonds by differentiating the free OH groups and the bound groups. It is a destructive method including the steps of methylation, hydrolysis, reduction with NaBD4, acetylation and analysis by mass spectrometry
• Example 2 preparation of branched maltodextrins from syrup rich in DP4: results
• the product obtained by this enzymatic treatment with the enzyme GT#19 contains significantly fewer ⁇ -1,4 bonds and more ⁇ -1,6 bonds than the starting point. The number of a-1,2 and a-1,3 bonds is not modified.
• the GT#19 enzyme is therefore an a-4,6 glucanotransferase.
• the GT#11 enzyme leads to a reduction in the percentage of ⁇ -1,4 bonds and the appearance of ⁇ -1,3 bonds.
• the digestibility of the product obtained by treatment with the GT#11 enzyme is also reduced (53 and 55%, for respective initial concentrations of 100 and 200 mg/mL, compared to 84 and 88% for untreated substrates).
• the mixture of a-glucans according to the present invention also presents an interesting in vitro digestibility profile according to the Englyst method.

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