Agent for correction of lactase deficiency

FIELD: medicine, biochemistry, pharmacy.

SUBSTANCE: invention relates to drugs used in treatment and prophylaxis of diseases associated with deficiency or absence of enzyme lactase in human body. Agent comprises enzyme lactase isolated from cultural fluid of microscopic fungus Penicillium canescens with activity 10000 U/g, not less, and shows stability in the pH range from 2.5 to 7.0 and temperatures from 4°C to 60°C. Agent provides effective cleavage of lactose in milk and dairy foodstuffs to a mixture of easily assimilable monosuccharides: glucose and galactose that results to availability of dairy foodstuffs for their using by humans suffering from lactose intolerance. Enzyme is stable that allows its using both for dosing orally with simultaneous using dairy foodstuffs and for their preliminary treatment.

EFFECT: valuable medicinal and nutrient properties of agent.

2 cl, 2 tbl, 2 dwg, 2 ex

 

The invention relates to medicines used for the treatment and prevention of diseases associated with disorders in persons suffering from lactose intolerance.

It is known (1)that the human digestive system contains a set of enzymes designed to break down complex nutrients into simpler molecules, in which they are absorbed in the human intestine. In particular, in the upper part of small intestine of man is synthesized by the enzyme lactase, which breaks down the disaccharide lactose contained in milk and dairy products in equimolar amounts of glucose and galactose, which are easily absorbed by the body (2).

Lactose intolerance (hypolactasia)caused by low levels or absence of the mucosa of the intestinal enzyme lactase, can occur in children and adults. The inability to break down lactose into glucose and galactose after consuming milk or dairy products is manifested by nausea, vomiting, bloating and abdominal pain, diarrhoea. At the same time, the exclusion from the diet of human milk and dairy products leads to certain violations of the regulatory systems of the body (especially in infant age) (2, 3).

Lactose intolerance in humans can be overcome in several ways:

- getting the low lactose or completely lactose-free milk by pre-hydrolysis of lactose in milk by using enzyme preparations,

- the use of drugs containing exogenous enzyme lactase microbial origin.

The first way is getting lactose-free milk, was introduced in the early 80-ies a number of companies ("Snam Progetti, Italy; "Gist-Brocades, the Netherlands). The disadvantage of this method is that it can only be used for processing of whole milk and unsuitable for processing dairy products (cottage cheese, cheese, yoghurt etc), because it leads to changes in their texture, appearance, and, in some cases, taste.

The second way is the use of pharmaceutical preparations containing the enzyme lactase microbial origin. These drugs are intended for oral use by people with lactase practically not produced or is produced is not enough in your own intestines.

Manufactured drugs, containing lactase, can be divided into two groups:

drugs, containing lactase, synthesized by yeast and bacteria with optimum action in the neutral and slightly alkaline zone pH;

drugs, containing lactase, synthesized by microscopic fungi with optimum action in the acidic zone pH.

The first group includes preparations "Lact-Aid", manufactured by "Sugar Co Lo. Pleantvi" (USA), "Maxilact" (firm "Gist Brocades, the Netherlands), "Lactaid" (firm "Sugar o"), "Lactozym" (firm "Novozymes"). All these preparations containing yeast lactase, are active in a fairly narrow range of pH (6.0 and 7.0) and no effect at pH below 6.0, which limits the scope of their use (4). These drugs are mainly used for processing of whole milk before drinking and ineffective in relation to lactose dairy products.

The second group includes drugs based lactis synthesized by microscopic fungi. These lactase active in the acidic zone pH (3,5-5,0) and, therefore, effective for hydrolysis of lactose dairy products and less effective in the hydrolysis of lactose whole milk. Thus, the firm "Fermentation Industries Kingstree (USA) received a lactase from Aspergillus niger and released in the form of a powder called "Lactrase-N"; company "Schwarz Pharma" makes the drug "Lactrase in capsule form on the basis of lactase from Aspergillus orysae(5, 6, 7).

Analysis of medications used for lactose intolerance, showed that for effective hydrolysis of lactose in milk and dairy products, you must use at least two kinds of products with optimum action in different pH zones.

The closest analogue to the proposed invention is to US patent No. 6,410,018 B1 Eisenhardt et al., which describes a composition for hydrolysis of lactose, consisting of two lactase of micron the descent with optimal actions in acidic and neutral zone pH (8). This, according to the authors, allows the best to carry out the hydrolysis of lactose by the consumption of milk and dairy products due to the fact that an enzyme works in the acidic environment of the stomach and the other in the human intestine at neutral and slightly alkaline pH values.

The disadvantage of the claimed compositions is the complexity and multi-stage cooking. The proposed mixture includes two enzyme preparation obtained from different producers with different technologies. The enzyme has optimum action in the neutral and slightly alkaline zone pH, covered with acid-resistant shell, then added lactase, the current in the acidic environment of the stomach, and the mixture is acid-soluble shell. The cooking process of the specified compositions a long time and requires additional material costs.

The technical result of the invention is to create a universal means for hydrolysis of lactose, able to work effectively both in acid and in neutral zone pH.

The technical result was achieved by obtaining highly purified enzyme lactase, isolated from the culture fluid of microscopic fungus Pen. canescens, with high enzymatic activity (at least 10,000 units/g) and specificity of action. Purified lactase (; -galactosidase, KF) has a molecular weight of 120-130 kD, an isoelectric point pI of 6.7, shows activity and stability in a wide pH range (2.5 to 7.0) and temperature (4-55° (C) (1, 2). The enzyme undergoes minor mixed type of inhibition by the products of hydrolysis of lactose that can be used in the process of a continuous hydrolysis of lactose.

These properties make the enzyme universal for operation at elevated temperature (37° (C)at room temperature and a temperature of 4°both in acid and in neutral zone pH.

The study of specific drug action of lactase was conducted on the most commonly consumed as food products (milk, yogurt, cottage cheese, yogurt). Processing of milk and dairy products was performed by the following doses of the enzyme: 500, 1000, 2000 and 4000 units per 100 g of product. The process is conducted at a temperature of 20°C for six hours, at a temperature of 4°C for 12 hours at 37°C for 2 hours with addition of gastric juice, simulating the internal environment of the organism.

In the course of research was chosen as the optimal dose of the enzyme that provides the necessary degree of hydrolysis of milk sugar (lactose). It was 2000 units per 100 g of fermented milk products and 4000 units per 100 g of whole milk. These concentrations of enzyme were used for p is Ogadenia further work.

When selecting a dose of lactase for pre-treatment of milk and dairy products before use, take into account the fact that for most people suffering from hypolactasia, some amount of lactose per day is acceptable. Use them on average 250 g milk products with a degree of hydrolysis of lactose 60-70% in a number of techniques does not lead to the manifestation of symptoms of lactose intolerance. Hydrolysis of lactose by 90% or more is required only in case of exceptional lactose (7, 9).

The invention is illustrated by the following examples.

Example 1.

In conical flasks with a capacity of 200 ml was placed 100 g of sediment was added to the enzyme with a total lactase activity 2000 units and 4000 units Contents of the cones were thoroughly stirred and kept at a temperature of 20°C. In the control experiment, the substrate was kept without added enzyme. For the comparative study of the action of the enzyme with foreign analogues used import drug Lactrase in the form of capsules with the same activity. Similarly prepared samples for processing milk in the refrigerator (4° (C) within 12 hours.

Determining formed during hydrolysis of glucose was carried out according to the method of G. Kurz, Beutler H.O.(10, 11, 12).

The results of the experiments for the pre-treatment of milk and dairy products, and t is the train comparative data of drug action with the action of imported similar Lactrase presented in table 1.

As can be seen from table 1, the degree of hydrolysis of lactose in milk by enzyme activity 2000 units at a temperature of 20°after 6 hours reaches 58%, and when using 4000 units - 65%. The same depth of hydrolysis can be achieved when processing milk appropriate doses at 4°With 12 hours.

In kefir, yogurt and cheese hydrolysis of lactose is faster and more deeply than milk due to the fact that dairy products have a pH of 4.0 to 4.5, close to the optimum actions proposed tools (4.0 to 4.5). 6 hours of treatment at room temperature (20° (C) or for 12 hours at 4°With a degree of hydrolysis of lactose in kefir and yogurt reaches 85 or 89 to 91% depending on the dose of applied drug. Lactose in the curd hydrolyzed in 97-100% after one hour of treatment at room temperature (20°and 100% after 12 hours at 4°C.

From table 1 also shows that the specific activity of the proposed tools is higher than that of imported drug Lactrase firm "Schwarz Pharma"as in the hydrolysis of lactose in milk (10-15%)and the hydrolysis of lactose in dairy products (5-10%).

Example 2.

To study the specific activity of the preparation of lactase in conditions that mimic the internal environment of the body, tapered cones together the awn 200 ml were placed 100 g of sediment, contributed enzyme with a total activity of lactase 2000 units and 4,000 units and added to 10 ml natural gastric juice "Equine" (10% by weight of the substrate) (1). The contents of the cones was mixed and placed in a thermostat at a temperature of 37°2 hours, shaking occasionally. In a trial experiment, the enzyme was added. As a comparison used the drug Lactrase in the same doses.

The processing time was limited to two hours, as from literature data it is known (13), the first clinical symptoms of lactase deficiency occurs in 1.5-2 h after consumption of milk and other dairy products. Samples were taken every 30 minutes. In them were determined by the glucose and used to calculate the degree of hydrolysis of lactose.

Data for the study the specific activity of the proposed tools in conditions that mimic the environment of the organism, are presented in table 2.

In conditions close to the conditions of the body (37°With, in the presence of gastric juice), the rate of hydrolysis of lactose was increased due to the temperature shift in the zone of optimal values of enzyme. Depending on the dose of applied drug lactose milk hydrolethalus 59% or 75% for 2 hours. During this same time, the degree of hydrolysis of lactose in kefir and yogurt were reached, respectively, 87 and 91%, and the cheese is already 1 hour was progeressive 94-100% lactose.

uravnitelny analysis of the specific actions proposed tools and Lactrase showed the proposed tool 5-15% efficient, especially in relation to lactose free milk.

Thus, the developed tool for the correction of a deficiency of lactase has a high specific activity against lactose milk and milk products, turning the milk sugar into the mixture of easily digestible sugars: glucose and galactose, thereby making dairy products available for people who suffer from lactase deficiency.

Pharmacokinetic studies conducted on 60 outbred rats-males, showed that the enzymatic activity of lactase in the blood plasma of experimental animals are not detected and the bulk of lactase activity (75%) is found in the feces.

To find the "model" for animal testing tools developed in vivo is not possible, since such pathology in animals have not been observed. The clean lines of animals with this pathology is not displayed. Given the lack of model laboratory animals with this pathology, the results of pharmacokinetics, testifying to the absence of specific activity of lactase in the blood plasma of experimental animals, and experience used in substitution treatment of imported products based on microbial lactase, testing offers the suggested medicines "in vivo" was not conducted.

Preclinical Toxicological studies offer funds held LLC OXFARM" on an experimental basis of the laboratory of pharmacology and chemotherapy GU NIINA them. Grause RAMS in accordance with the "Manual on experimental (preclinical) study of new pharmacological substances", 2000 (14). Study of acute toxicity of the proposed funds spent on healthy outbred rats male and mice-males SHK showed that the drug belongs to low-toxic substances: indicator of acute toxicity (LD50) mice were at 3250 mg/kg MTD (LD10) - 1710 mg/kg; in rats LD50was 2970 mg/kg; MTD - 1563 mg/kg In the study of chronic toxicity on healthy outbred rats male was found that the introduction of the drug lactase inside the test animals in a therapeutic, 2-fold and 5-fold doses did not lead to the violation of the functional state of the organism of experimental animals and did not cause changes of peripheral blood counts, biochemical blood indices, morphological structure of tissues and organs. The drug has no, anaphylactogenic and immunotoxic properties, does not affect the basic parts of humoral and cellular immunity, does not have teratogenic and embryotoxic effects.

On the basis ol stavlennii in the Ministry of health of the Russian Federation documentation was received permission to conduct clinical trials of the drug.

References

1. Halperin, S. the Physiology of man and animals, M., 1970.

2. Valenkevich LN. // Clinical medicine, 1996, No. 8.

3. Korshunov F, Darkina E.E. // Pediatrics, 1997, No. 3.

4. Coughlin R.W., Charles M. - In: Immobilized Enzymes for Food Processing / Ed.W.Pitcher - Florida: USA, CRC Press, 1980, p.153-173; Itoh T., Suzuki M., Adachi S/ - Agric. Biol. Chem., 1982, v.46, No.4, p.899-904.

5. Green M.L. // Milk Industry, 1980, v.82, N 3, p.25-31.

6. Collins M.S., Di Palma Y.A., Pierson W.P. et al. // Gastroenterology - 1986 - vol.90 - p.1377-1378.

7. Di Palma Y.A., Collins M. S. // J. Clin. Gastroenterol. - 1989 - vol.11, No. 3 - p.290-293.

8. U.S. patent No. 6,410,018 B1 dated June 25, 2002

9. Moskovitz, M., Curtis, C., Gavaler Y. // Am.J. Gastroenterol. - 1987 - vol.82, No. 7 - R-635/

10. Kurz G. & K. Wallenfels Methods der enzymatischen Analyse (Bergmeyer H.U., Hrsg.) 3.Aufl., Bd.2, S.1225-1229 and S.1324-1327, Verlag Chemie, Weinheim, and (1974) in Methods of Enzymatic Analysis (Bergmeyer, H.U., ed.) 2nd., vol.3, pp.1180-1184 and pp.1279-1282, Verlag Chemie, Weinheim, Academic Press, Inc. New York and London.

11. Beutler H.O. Methods der enzymatischen Analyse (Bergmeyer H.U., ed.), 3rd ed., Vol.VI, pp.104-112, Verlag Chemie, Weinheim, Deerfield Beach/Florida, Basel.

12. Methods of Biochemical Analysis and Food Analysis. Instruction for the Analysis of Foodstuffs in Research, Production and Official Control. Boehringer Mannheim GmbH, 1989, p.86-88.

13. Kozlovsky A.A. // Honey. News, 2001, No. 1.

14. Manual on experimental (preclinical) study of new pharmacological substances. Moscow, 2000

1. Means for correcting a deficiency of lactase, representing a highly purified enzyme lactase, wherein the lactase selected from the culture fluid mushroom producer Penicilium canescens, is fully active not less than 10,000 units/g and stable in a wide pH range (2.5 to 7.0) and temperature (from 4 to 60° C).

2. The tool according to claim 1, characterized in that it is able to break down milk sugar into a mixture of digestible monosaccharides: glucose and galactose, as the oral application and preliminary processing of milk and dairy products before use.



 

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