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Kefir production method

Kefir production method
IPC classes for russian patent Kefir production method (RU 2510999):
A23C9/127 -
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/ 2258381
/ 2260978
/ 2265361
/ 2266008
/ 2266322
/ 2270586
/ 2272548
/ 2279807
/ 2286062
/ 2287944

FIELD: food industry.

SUBSTANCE: method involves standardisation, pasteurisation, homogenisation, cooling to fermentation temperature, introduction of kefir fungi based industrial starter in an amount of 2% simultaneously with transglutaminase enzyme in an amount of 0.2 kg per 1000 kg of the standardised mixture at a temperature of 23-25°C, ripening, cooling to maturation temperature, bottling. The content of lactoferrin in the ready product is 500-1100 mg/l.

EFFECT: invention allows to enhance the product biological value and prophylactic properties, prevent synaeresis in the process of storage, enhance the product rheological properties, produce a product with improved structurem and enhanced quality, a milder fermented milk taste and aroma, impart creaminess to the product and extend its storage life.

1 ex

 

The invention relates to food industry, in particular breast, and can be used in the manufacture of yogurt.

A known method for the production of yogurt, including pasteurization of milk, homogenization, cooling, fermentation of kefir fungi that were pre-cultivated in milk at a ratio of 1:10-1:50. Then conduct the fermentation at temperatures of 18-30°C for 6-18 hours, maturing at 10-18°C for 12 to 48 hours (see EN 2279807, 20.07.2006).

Disadvantages - low organoleptic and physico-chemical characteristics, small shelf life of the product.

The technical result of the invention is the prevention of syneresis during storage, improving the rheological properties of the product, a product with improved structure and high quality, with more soft cheese taste and aroma, giving slivochnoi product.

The technical result is achieved by a method for the production of yogurt includes standardization, pasteurization, homogenization, cooling to a temperature of fermentation, making the production of yeast in kefir fungi, fermentation, cooling to a temperature of maturation, bottling, characterized in that after cooled to the fermentation temperature, simultaneously with the production leaven on kefir fungi, the number of which SOS is defaults to 2% by weight normalized mixture, make the enzyme transglutaminase in the amount of 0.2 kg per 1000 kg normalized mixture at a temperature of 23-25°C, the concentration of lactoferrin in the final product ranges from 500 to 1100 mg/L.

The enzyme transglutaminase is involved in the formation of additional bonds in protein molecules, leading to the binding of protein molecules. Transglutaminase catalyzes the reaction of acyl transfer between γ-carboxyamide group of the glutamine residue of a protein or peptide (acyl donor) and the primary amino groups of various amino compounds (acyl acceptor), including the ε-amino group of a lysine residue of the peptide by the reaction:

As a result of binding residues of peptides or proteins, glutamine and lysine are formed of high-molecular compounds containing ε-(γ-glutamyl)-lysine intra - and intermolecular isopeptide communication. The formation of these relationships has an impact on the structure and functional properties of proteins.

Binding proteins by transglutaminase causes the increase of the viscosity of the product, lowering the degree of syneresis, achieving a smooth surface, reducing production costs, as in the milk mixture does not require payment of skimmed milk powder to improve consistency by increasing protein content.

The proposed method is carried out as the way. Raw milk normalize, homogenized, pasteurized, cooled to the fermentation temperature of 23-25°C, making the production leaven on kefir fungi in the amount of 2% by weight normalized mixture and the enzyme transglutaminase at the rate of 0.2 kg per 1000 kg normalized mixture, sours it for 8-10 hours until the formation of a clot, active acidity which is 4.50-4,55% pH, partially cooled to a temperature of 18-20°C and stirred curd is cooled to a temperature of 4-8°C, poured into consumer packaging sent to dokladnie and maturation at a temperature of 2-6°C for 12 hours, you get a finished product with the content of lactoferrin from 500 to 1100 mg/L.

Sign concerning what the content of lactoferrin in the product ranges from 500 to 1100 mg/l, due to the joint action of microorganisms kefir starter and the enzyme transglutaminase.

The biochemical pathways by which the synthesis of lactoferrin in microorganisms, similar to those in other organisms. Installed capacity of kefir grains, representing a mixture of lactic acid bacteria p.p.Lactococcus, Lactobacillus and Saccharomyces lactis to the synthesis of its own bacterial lactoferrin (BLF). Bacteria kefir starter culture actively developing their own siderophore, including bacterial lactoferrin. When the volume synthesis of siderophores bacteria is a limiting factor in their survival outside the host, that is, the microbes are not able to synthesize their own siderophore, actively use molecules present in the host organism; they are completely dependent upon him and not being able to successfully evolve and survive in the environment. The introduction of the mixture of the enzyme transglutaminase activates the bacteria's ability to synthesize its own lactoferrin for their survival. Transglutaminase catalyzes the formation of covalent bonds between free amino groups (free or from the side chains of lysine and the gamma carboxamide groups of glutamine. The covalent bond formed by transglutaminase resistant to proteolysis. Specific isopeptide arise between proteins. Bonds are formed within the protein and between individual molecules. Transglutaminase acts exclusively on proteins. Catalyzed by mediated through glutaraldehydes deamination of natural amino acids and the biosynthesis of amino acids. Transglutaminase catalyzes the transfer reaction of acyl Y-carboxylamide groups in the peptide chain of the protein. When the enzyme interacts with protein, it may be the formation of cross-links ∈(Y-Glu)-Lys and the substitution of Gln for Glu in the result of desametasone.

The specificity of transaminases is provided by the protein component. The enzyme catalyzes re the OS NH 2groups not on the α-ketoacid, and first to coenzyme a pyridoxal phosphate. The resulting intermediate compound (Chippewa base) undergoes intramolecular transformations (labilization of the α-hydrogen atom, the energy redistribution communication), leading to the release of α-ketoacids and pyridoxalphosphate; the latter in the second stage of the reaction reacts with any other α-ketokislot that through the same stages of the formation of intermediate compounds (going in the opposite direction) leads to the synthesis of new amino acids and the release of pyridoxal phosphate. Due to the fact that all transaminases carbonyl group of the coenzyme (-CHO) is linked to the ε-amino group of lysine a protein part, the interaction between the substrate, i.e. the L-amino acid and pyridoxal phosphate, is not by condensation with the release of water molecules, and by substitution reactions, in which the NH2group of the substrate displaces ε-NH2-lysine group in the molecule of enzyme protein, which leads to the formation pyridoxalphosphate complex. All or nearly all of the natural amino acids (except methionine) first react with α-Ketoglutarate acid transamination reaction with the formation of glutamic acid and the corresponding keto acid. The resulting glutamic acid is then subjected to direct the oxidative deamination under the action of glutamate dehydrogenase. Because both reactions (transamination and deamination of glutamic acid) are reversible, the conditions for the synthesis of essentially any amino acid, if you have the appropriate α-keto acid. Thus, transglutaminase catalyzes mediated through glutaraldehydes deamination of natural amino acids and the synthesis of new amino acids. With the active action of the enzyme, which is expressed in the increased formation of new molecules of amino acids, the activation reactions of anabolism in microbial associations, which leads to an increase of lactoferrin in the finished product.

The proposed technology of production of kefir making transglutaminase, enables the generation of a native lactoferrin microorganisms in the composition of kefir grains in an amount of from 500 to 1100 mg/l compared to control up to 300 mg/L.

An example of the method.

Example

The original milk normalize by the mass fraction of fat, homogenized at a pressure of 17 MPa at a temperature of 55-60°C, pasteurized at a temperature of 94-96°C with a holding time of 300 seconds, cooled to the fermentation temperature of 23-25°C, making the production leaven on kefir fungi in the amount of 2% by weight normalized mixture and the enzyme transglutaminase at the rate of 0.2 kg per 1000 kg normalized mixture, sours during the 8-10 hours before the formation of a clot active acidity 4,50-4,55, partially cooled to a temperature of 18-20°C and stirred curd is cooled to a temperature of 4-8°C, poured into consumer packaging, send in a locker on dokladnie and maturation at a temperature of 2-6°C for 12 hours. Get the finished product with the content of lactoferrin from 500 to 1100 mg/L.

Organoleptic characteristics of kefir obtained by example: the consistency of a homogeneous, dense, moderately dense, taste and smell clean milk, microbiological indicators performed according to the requirements of Federal law.

The proposed method of production of yogurt allows you to:

- to obtain a product of high quality by improving the rheological properties of the product;

to improve organoleptic characteristics;

- to give the product slivochnoi;

- exclude the addition of skimmed milk powder to improve consistency by increasing the protein in the finished product;

- use it in the power of all age groups;

to increase the shelf life of the finished product up to 14 days by reducing the degree of syneresis during storage at a storage temperature of 2-6°C.

Method for the production of yogurt, including standardization, pasteurization, homogenization, cooling to a temperature of fermentation, making the production of yeast in kefir fungi, fermentation, chilled the f to a temperature of ripening, bottling, wherein after cooling to fermentation temperature, simultaneously with the production leaven on kefir fungi, which amount is 2%, making the enzyme transglutaminase in the amount of 0.2 kg per 1000 kg normalized mixture at a temperature of 23-25°C, the concentration of lactoferrin in the finished product is 500-1100 mg/L.

 

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