WO2014165030A2 - Process for enhancing the amylase inhibitory efficacy from phaseolus vulgaris extracts - Google Patents

Process for enhancing the amylase inhibitory efficacy from phaseolus vulgaris extracts Download PDF

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Publication number
WO2014165030A2
WO2014165030A2 PCT/US2014/024176 US2014024176W WO2014165030A2 WO 2014165030 A2 WO2014165030 A2 WO 2014165030A2 US 2014024176 W US2014024176 W US 2014024176W WO 2014165030 A2 WO2014165030 A2 WO 2014165030A2
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Prior art keywords
solution
amylase
alpha
bean extract
particles
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PCT/US2014/024176
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French (fr)
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WO2014165030A3 (en
Inventor
Robert J. SARAMA
Gregory ARCUINO
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Sunny Delight Beverages Company
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Publication date
Application filed by Sunny Delight Beverages Company filed Critical Sunny Delight Beverages Company
Priority to EP14717923.8A priority Critical patent/EP2970404A2/en
Priority to MX2015011499A priority patent/MX2015011499A/en
Priority to RU2015143561A priority patent/RU2015143561A/en
Priority to CA2900472A priority patent/CA2900472A1/en
Priority to JP2016501431A priority patent/JP2016517413A/en
Priority to CN201480013635.3A priority patent/CN105008392A/en
Priority to BR112015021588A priority patent/BR112015021588A2/en
Publication of WO2014165030A2 publication Critical patent/WO2014165030A2/en
Publication of WO2014165030A3 publication Critical patent/WO2014165030A3/en
Priority to HK16104463.2A priority patent/HK1216539A1/en

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    • 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.)
    • C12N9/2422—Alpha-amylase (3.2.1.1.) from plant source
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P3/00—Drugs for disorders of the metabolism
    • A61P3/04—Anorexiants; Antiobesity agents
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P3/00—Drugs for disorders of the metabolism
    • A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
    • A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
    • 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

  • Amylase is an enzyme responsible for breaking down the main source of carbohydrates in the human diet, namely, starch.
  • the digestion of starch begins in the mouth where alpha-amylase present in saliva hydrolyzes glucosidic bonds of starch. By the time thoroughly chewed food reaches the stomach, the average chain length of starch is reduced from several thousand to less than eight glucose units.
  • the acid level in the stomach inactivates the salivary alpha-amylase. Further digestion of starch continues in the small intestine by pancreatic alpha- amylase, which is similar to salivary alpha-amylase.
  • Amylase inhibitors are derived from various sources, including
  • Lipoprotein complexes which comprise an amylase-inhibiting protein together with a phospholipid (such as phosphatidylcholine). These complexes are said to be useful in treating hypercholesterolemia.
  • phaseolamin extract is said to be safe and suitable for consumption by man and animals.
  • alpha-amylase begins the process of the enzymatic
  • the present invention relates to a method for purifying bean extract alpha-amylase material, comprising the steps of: [0012] (a) suspending the alpha-amylase material in an aqueous solution at a pH of from about 3.0 to about 3.5;
  • the basic invention herein is a process that improves upon known processes for the purification of an alpha-amylase inhibitor from white kidney beans (Phaseolus vulgaris), that provides a product which has the following properties:
  • an alpha-amylase inhibitor which provides a clear solution with no turbidity, settling, or bean flavor
  • an alpha-amylase inhibitor which can be easily incorporated into water, clear beverages, teas, etc. for the purpose of weight control.
  • the commercial bean extract powder of the process described in U.S. Published Patent Application 2006/0147565, incorporated herein by reference was suspended in an aqueous solution containing a carboxylic acid or carboxylic acid salt (such as citric acid, malic acid and/or tartaric acid, or citrate, malate or tartrate salts) to carefully adjust the solution pH to from about 3.0 to about 3.5, such as from about 3.3 to about 3.5.
  • a carboxylic acid or carboxylic acid salt such as citric acid, malic acid and/or tartaric acid, or citrate, malate or tartrate salts
  • a preservative such as benzoates, sorbates, sodium hexametaphosphate (SUMP), or dimethyl dicarbonate (DMDC) was added, and the mixture was heated to from about 175F to about 195F, such as about 180 ⁇ 2F for from about 10 to about 120 seconds, such as from about 10 to about 60 seconds (preferably from about 10 to about 20 seconds).
  • This solution was then cooled and kept at from about 65 to about 85F, such as from about 75 to about 85F, to allow time for the bean extract particles to settle.
  • An extraction time of from about 3 hours to about 24 hours, such as from about 12 to about 24 hours, under static non-agitated conditions, is needed for the extraction to occur.
  • the supernatant is then separated from the bean extract particles (such as by decanting).
  • the amylase inhibiting protein is found in the liquid phase.
  • the protein can be concentrated through reverse osmosis or by gentle drying, but the protein must be maintained in solution during those processes.
  • the pH of the final extract solution, as well as the specific carriers utilized, can be adjusted to from about 3.0 to about 3.5;
  • Phaseolus vulgaris such as kidney beans, cranberry beans, black turtle beans, flageolet, white beans, and yellow beans, or other genetically modified cultivars.
  • One gram of white kidney bean extract is added to a 470 gram mixture containing 0.040 wt% sodium hexametaphosphate, 0.015 wt% citric acid, 0.009 wt% potassium sorbate, 0.009 wt% sodium benzoate and water.
  • the mixture is heated to 180F for 15 seconds and cooled to 85F for 24 hours.
  • a 5 cc aliquot sample is removed for alpha amylase inhibition testing.
  • Two companion control samples are also prepared and sampled for alpha amylase inhibition testing.
  • the first control sample is prepared by adding 1 gram of white kidney bean extract to 470 grams of water, heating it to 180F for 15 seconds and holding it at 85F for 24 hours.
  • the second control consists of water and all of the components (salts) as found in the rest sample. Results of amylase testing shows that the test sample provides significantly more amylase inhibition than the control samples, on the order of lOx greater.

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Genetics & Genomics (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Wood Science & Technology (AREA)
  • Zoology (AREA)
  • Medicinal Chemistry (AREA)
  • Biochemistry (AREA)
  • Botany (AREA)
  • Molecular Biology (AREA)
  • General Engineering & Computer Science (AREA)
  • Diabetes (AREA)
  • Biomedical Technology (AREA)
  • Microbiology (AREA)
  • Biotechnology (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Biophysics (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Veterinary Medicine (AREA)
  • Public Health (AREA)
  • Animal Behavior & Ethology (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • General Chemical & Material Sciences (AREA)
  • Obesity (AREA)
  • Hematology (AREA)
  • Endocrinology (AREA)
  • Emergency Medicine (AREA)
  • Child & Adolescent Psychology (AREA)
  • Medicines Containing Plant Substances (AREA)
  • Peptides Or Proteins (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Medicinal Preparation (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

An improved method of purifying bean extract alpha-amylase material is disclosed. The materials purified by this process provide significantly more amylase inhibition than materials purified by other processes. In this process: (a) bean extract alpha-amylase material is suspended in an aqueous solution at a solution pH of from about 3.0 to about 3.5; (b) a preservative is added to the solution; (c) the solution is heated to about 175F to about 195F for from about 10 to about 120 seconds; (d) the solution is cooled to a temperature of from about 65 to about 85F, and the solution is allowed to sit, under static non-agitated conditions, at a temperature with that defined range for from about 3 to about 24 hours to allow bean extract particles to settle out of solution; and (e) the particles are separated from the supernatant.

Description

PROCESS FOR ENHANCING THE AMYLASE
INHIBITORY EFFICACY FROM PHASEOLUS VULGARIS EXTRACTS
Background
[0001] Amylase is an enzyme responsible for breaking down the main source of carbohydrates in the human diet, namely, starch. The digestion of starch begins in the mouth where alpha-amylase present in saliva hydrolyzes glucosidic bonds of starch. By the time thoroughly chewed food reaches the stomach, the average chain length of starch is reduced from several thousand to less than eight glucose units. The acid level in the stomach inactivates the salivary alpha-amylase. Further digestion of starch continues in the small intestine by pancreatic alpha- amylase, which is similar to salivary alpha-amylase.
[0002] Decreasing the absorption of carbohydrates by inhibiting the digestion of starch is a very promising strategy in the fields of, for example, weight loss and diabetes mellitus. From a dietary standpoint, it is important to target the breakdown of starch since starch is a relatively non-essential nutrient, which provides calories with little benefit.
[0003] Amylase inhibitors are derived from various sources, including
vegetable albumins and leguminous plants. Currently, extracts from beans are being utilized most often as a source of amylase inhibitors.
[0004] Current methods for purification of amylase inhibitors, which include concentrating and drying beans, include the use of heat treatments and/or solvents. See, for example, U.S. Patent 6,340,699, Cestaro et al, issued January 22, 2002. However, the use of heat treatments and/or solvents has several drawbacks. For example, at high temperatures, certain heat sensitive components of the amylase inhibitor from beans can become degraded. As a result, the amylase inhibitor exhibits a decrease in both stability and potency. In addition, there can be environmental and health concerns associated with the use of solvents during such purification processes. For example, extraction of amylase inhibitors from beans using solvents can result in residual contamination of the extract with the toxic solvent. Furthermore, disposal of the large quantities of solvent required during purification processes can raise environmental concerns.
[0005] Examples of such amylase inhibitor purification processes are as
follows:
[0006] U.S. Patent 6,340,669, Cestaro et al (assigned to Hunza di Maria
Carmela Marazzita S.A.S.), issued January 22, 2002, describes lipoprotein complexes which comprise an amylase-inhibiting protein together with a phospholipid (such as phosphatidylcholine). These complexes are said to be useful in treating hypercholesterolemia.
[0007] U.S. Published Patent Application 2006/0147565, Skop et al (assigned to Pharmachem Laboratories, Inc.), published July 6, 2006, describes the extraction and purification of amylase inhibitors from white beans using supercritical carbon dioxide processes under vacuum pressure. A method for inducing weight loss using the purified amylase inhibitors is also taught.
[0008] U.S. Published Patent Application 2009/0042779, Bollini et al,
published February 12, 2009, defines the use of beans, which are bred to be essentially free from phytohemagglutinin, for extracting amylase inhibitors, as well as the combination of that extract with phaseolamin. The described highly purified phaseolamin extract is said to be safe and suitable for consumption by man and animals.
[0009] U.S. Published Patent Application 2009/0169657, Berlanda et al, published July 2, 2009, describes the use of hydro-ethanolic mixtures on suitably concentrated aqueous extracts of kidney beans to produce enriched extracts with an alpha-amylase inhibitor content having an activity between 1,000 and 1,600 USP/mg and a phytohaemagglutinin content between 8,000 and 30,000 HAU/g. It is said that this extract can be formulated for diet use at relatively low doses.
[0010] In the mouth, alpha-amylase begins the process of the enzymatic
digestion of starch, a main source of carbohydrates in the human diet. Proteinaceous amylase inhibitors from Phaseolus vulgaris (white kidney bean) varieties have been known for some time. Decreasing the absorption of carbohydrates by blocking starch digestion through the inhibition of amylase can aid in the control of weight gain or diabetes mellitus. To achieve this end, methods have been developed to extract amylase inhibitors from beans in order to allow the incorporation of said inhibitors into dietary supplements. Current methods for the extraction and purification of amylase inhibitors from beans have not been totally satisfactory in terms of processes that involve harsh heat and solvent treatments which yield amylase inhibitors having impurities and/or less than full activity. U.S. Published Patent Application 2006/0147565, discussed above, describes a process for purifying the amylase inhibitor from white kidney beans that is claimed to be more potent than the amylase inhibitors derived from conventional methods employing heat and solvents. Surprisingly, it has been discovered that the amylase inhibitor extract powder as processed by the methods described in the '565 patent application can be further improved by an additional process step. The result is a clear, stable, tasteless aqueous mixture which contains the amylase inhibiting protein having a significant increase (as much as tenfold) in activity.
Summary
[0011] The present invention relates to a method for purifying bean extract alpha-amylase material, comprising the steps of: [0012] (a) suspending the alpha-amylase material in an aqueous solution at a pH of from about 3.0 to about 3.5;
[0013] (b) adding a preservative to the solution;
[0014] (c) heating the solution to from about 175F to about 195F for from
10 to about 120 seconds;
[0015] (d) cooling the solution to a temperature of from about 65 to about
85F and letting the solution sit, under static non-agitated conditions, at a temperature within the defined range for from about 3 to about 24 hours to allow bean extract particles to settle out of solution; and
[0016] (e) separating the particles from the supernatant (such as by
decanting the supernatant).
[0017] All percentages and ratios given herein are "by weight" unless
otherwise specified. All patents and other documents discussed herein are incorporated herein by reference.
Detailed Description
[0018] The basic invention herein is a process that improves upon known processes for the purification of an alpha-amylase inhibitor from white kidney beans (Phaseolus vulgaris), that provides a product which has the following properties:
[0019] (1) an alpha-amylase inhibitor that is up to ten times more
efficacious than commercially available bean extracts,
[0020] (2) an alpha-amylase inhibitor which is stable when maintained in an aqueous solution;
[0021] (3) an alpha-amylase inhibitor which provides a clear solution with no turbidity, settling, or bean flavor; and [0022] (4) an alpha-amylase inhibitor which can be easily incorporated into water, clear beverages, teas, etc. for the purpose of weight control.
[0023] In an effort to produce a clarifying solution of alpha-amylase inhibitor from bean extract being produced by the method described in U.S. Published Patent Application 2006/0147565, it was surprisingly discovered that the clarifying process resulted in not only clarifying the bean abstract solution, but in also increasing the amylase inhibitory efficacy tenfold over the starting material. Further, it has been observed that the inhibiting protein is more stable in that solubilized state.
[0024] In order to achieve this, the commercial bean extract powder of the process described in U.S. Published Patent Application 2006/0147565, incorporated herein by reference, was suspended in an aqueous solution containing a carboxylic acid or carboxylic acid salt (such as citric acid, malic acid and/or tartaric acid, or citrate, malate or tartrate salts) to carefully adjust the solution pH to from about 3.0 to about 3.5, such as from about 3.3 to about 3.5. A preservative, such as benzoates, sorbates, sodium hexametaphosphate (SUMP), or dimethyl dicarbonate (DMDC) was added, and the mixture was heated to from about 175F to about 195F, such as about 180 ± 2F for from about 10 to about 120 seconds, such as from about 10 to about 60 seconds (preferably from about 10 to about 20 seconds). This solution was then cooled and kept at from about 65 to about 85F, such as from about 75 to about 85F, to allow time for the bean extract particles to settle. An extraction time of from about 3 hours to about 24 hours, such as from about 12 to about 24 hours, under static non-agitated conditions, is needed for the extraction to occur. The supernatant is then separated from the bean extract particles (such as by decanting). The amylase inhibiting protein is found in the liquid phase. The protein can be concentrated through reverse osmosis or by gentle drying, but the protein must be maintained in solution during those processes.
[0025] The above-described process can be varied in at least the following manner:
[0026] (1) additional purification of the solution can be carried out by reverse osmosis or forms of membrane filtration;
[0027] (2) the pH of the final extract solution, as well as the specific carriers utilized, can be adjusted to from about 3.0 to about 3.5; and
[0028] (3) the process can be carried out using extracts from other
varieties of Phaseolus vulgaris, such as kidney beans, cranberry beans, black turtle beans, flageolet, white beans, and yellow beans, or other genetically modified cultivars.
[0029] All references, patents and patent applications cited herein are
incorporated in this application by reference, unless otherwise stated.
Example
[0030] One gram of white kidney bean extract is added to a 470 gram mixture containing 0.040 wt% sodium hexametaphosphate, 0.015 wt% citric acid, 0.009 wt% potassium sorbate, 0.009 wt% sodium benzoate and water. The mixture is heated to 180F for 15 seconds and cooled to 85F for 24 hours. A 5 cc aliquot sample is removed for alpha amylase inhibition testing.
[0031] Two companion control samples are also prepared and sampled for alpha amylase inhibition testing. The first control sample is prepared by adding 1 gram of white kidney bean extract to 470 grams of water, heating it to 180F for 15 seconds and holding it at 85F for 24 hours. The second control consists of water and all of the components (salts) as found in the rest sample. Results of amylase testing shows that the test sample provides significantly more amylase inhibition than the control samples, on the order of lOx greater.

Claims

What is claimed is:
1. A method of purifying bean extract alpha-amylase material, comprising the steps of:
(a) suspending said material in an aqueous solution at a solution pH of from about 3.0 to about 3.5;
(b) adding a preservative to the solution;
(c) heating the solution to about 175F to about 195F, for from about 10 to about 120 seconds;
(d) cooling the solution to a temperature of from about 65 to about 85F and letting the solution sit, under static non-agitated conditions, at a temperature within that defined range for from about 3 to about 24 hours to allow bean extract particles to settle out of the solution; and
(e) separating the particles from the supernatant.
2. The method of claim 1 wherein, in step (a), a carboxylic acid or carboxylic acid salt is used to adjust the solution pH.
3. The method according to claim 1 wherein, in step (b), the preservative is selected from benzoates, sorbates, SHMP, DMDC, and mixtures thereof.
4. The method according to claim 1 wherein the heating in step (c) takes place for about 10 to about 20 seconds.
5. The method according to claim 1 wherein, in step (d), the solution is
concentrated using reverse osmosis or gentle drying, while the alpha-amylase material is maintained in solution.
6. The method according to claim 1 wherein the bean extract alpha-amylase material used in step (a) is obtained by a supercritical carbon dioxide process carried out under vacuum pressure.
7. The method according to claim 1 wherein, in step (e), the particles are separated out by decanting the supernatant.
8. The method according to claim 2 wherein the carboxylic acid is citric acid or a citrate salt.
9. The method according to claim 3 wherein the preservative is sodium benzoate.
10. The purified bean extract alpha-amylase material prepared according to the method of claim 1.
PCT/US2014/024176 2013-03-13 2014-03-12 Process for enhancing the amylase inhibitory efficacy from phaseolus vulgaris extracts WO2014165030A2 (en)

Priority Applications (8)

Application Number Priority Date Filing Date Title
EP14717923.8A EP2970404A2 (en) 2013-03-13 2014-03-12 Process for enhancing the amylase inhibitory efficacy from phaseolus vulgaris extracts
MX2015011499A MX2015011499A (en) 2013-03-13 2014-03-12 Process for enhancing the amylase inhibitory efficacy from phaseolus vulgaris extracts.
RU2015143561A RU2015143561A (en) 2013-03-13 2014-03-12 METHOD FOR INCREASING EFFICIENCY OF AMILASE INHIBITION WITH APPLICATION OF ORDINARY BEAN EXTRACTS
CA2900472A CA2900472A1 (en) 2013-03-13 2014-03-12 Process for enhancing the amylase inhibitory efficacy from phaseolus vulgaris extracts
JP2016501431A JP2016517413A (en) 2013-03-13 2014-03-12 Method for enhancing amylase inhibitory effect of common bean extract
CN201480013635.3A CN105008392A (en) 2013-03-13 2014-03-12 Process for enhancing the amylase inhibitory efficacy from phaseolus vulgaris extracts
BR112015021588A BR112015021588A2 (en) 2013-03-13 2014-03-12 process for improving amylase inhibitory efficacy from phaseolus vulgaris extracts
HK16104463.2A HK1216539A1 (en) 2013-03-13 2016-04-19 Process for enhancing the amylase inhibitory efficacy from phaseolus vulgaris extracts

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
US201361779584P 2013-03-13 2013-03-13
US61/779,584 2013-03-13
US14/204,622 2014-03-11
US14/204,622 US9290752B2 (en) 2013-03-13 2014-03-11 Process for enhancing the amylase inhibitory efficacy from phaseolus vulgaris extracts

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WO2014165030A2 true WO2014165030A2 (en) 2014-10-09
WO2014165030A3 WO2014165030A3 (en) 2014-12-04

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EP (1) EP2970404A2 (en)
JP (1) JP2016517413A (en)
CN (1) CN105008392A (en)
BR (1) BR112015021588A2 (en)
CA (1) CA2900472A1 (en)
HK (1) HK1216539A1 (en)
MX (1) MX2015011499A (en)
RU (1) RU2015143561A (en)
WO (1) WO2014165030A2 (en)

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Publication number Priority date Publication date Assignee Title
US11096978B2 (en) 2018-01-12 2021-08-24 Mellitas Health Foods, LLC Common bean (phaseolus vulgaris) extract with high a-amylase inhibitory activity and low hemagglutinin activity

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6340699B1 (en) 1998-05-01 2002-01-22 Eli Lilly And Company SPLA2 inhibitor compounds for treatment of disease
US6340669B1 (en) 1999-01-22 2002-01-22 Hunza Di Maria Carmela Marazzita S.A.S. Lipoprotein complexes and compositions containing them
US20060147565A1 (en) 2002-06-28 2006-07-06 Pharmachem Laboratories, Inc. Purified amylase inhibitor and novel process for obtaining the same
US20090042779A1 (en) 2004-03-30 2009-02-12 Roberto Bollini Purified Extract of an Alpha-Amylase Inhibitor From Phytoemagglutinin-Essentially Free Beans, Process for Its Extraction and Compositions Containing It
US20090169657A1 (en) 2005-12-22 2009-07-02 Davide Berlanda Phaseolus vulgaris extracts, their use, and formulations containing them

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6340699B1 (en) 1998-05-01 2002-01-22 Eli Lilly And Company SPLA2 inhibitor compounds for treatment of disease
US6340669B1 (en) 1999-01-22 2002-01-22 Hunza Di Maria Carmela Marazzita S.A.S. Lipoprotein complexes and compositions containing them
US20060147565A1 (en) 2002-06-28 2006-07-06 Pharmachem Laboratories, Inc. Purified amylase inhibitor and novel process for obtaining the same
US20090042779A1 (en) 2004-03-30 2009-02-12 Roberto Bollini Purified Extract of an Alpha-Amylase Inhibitor From Phytoemagglutinin-Essentially Free Beans, Process for Its Extraction and Compositions Containing It
US20090169657A1 (en) 2005-12-22 2009-07-02 Davide Berlanda Phaseolus vulgaris extracts, their use, and formulations containing them

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CN105008392A (en) 2015-10-28
US9290752B2 (en) 2016-03-22
CA2900472A1 (en) 2014-10-09
EP2970404A2 (en) 2016-01-20
US20140273157A1 (en) 2014-09-18
RU2015143561A (en) 2017-04-19
BR112015021588A2 (en) 2017-07-18
WO2014165030A3 (en) 2014-12-04
HK1216539A1 (en) 2016-11-18
MX2015011499A (en) 2017-03-27

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