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> Chemicals & Drugs > Amino Acid > Amylase

Amylase

Amylase is a critical enzyme involved in the breakdown of starch and glycogen, playing a vital role in carbohydrate metabolism.
This enzyme catalyzes the hydrolysis of alpha-1,4-glucosidic bonds, converting complex polysaccharides into simpler sugars.
Amylase is found in various organisms, including humans, animals, plants, and microorganisms, and is essential for proper digestion and energy production.
Researchers studying amylase can leverage PubCompare.ai's AI-driven platform to effortlessly locate the best protocols from literature, preprints, and patents, ensuring reproducibility and accuracy in their amylase research.
Explort the power of data-driven comparisons to enhance your research outcomes and advance our understanding of this important enzyme.

Most cited protocols related to «Amylase»

1
α-Amylase Inhibition Assay of A. pavonina Leaf Extract
Cited 25 times
The α-amylase inhibition assay was performed using the 3,5-dinitrosalicylic acid (DNSA) method [8 (link)]. The leaf extract of A. pavonina was dissolved in minimum amount of 10% DMSO and was further dissolved in buffer ((Na2HPO4/NaH2PO4 (0.02 M), NaCl (0.006 M) at pH 6.9) to give concentrations ranging from 10 to 1000 μg/ml. A volume of 200 μl of α-amylase solution (2 units/ml) was mixed with 200 μl of the extract and was incubated for 10 min at 30 °C. Thereafter 200 μl of the starch solution (1% in water (w/v)) was added to each tube and incubated for 3 min. The reaction was terminated by the addition of 200 μl DNSA reagent (12 g of sodium potassium tartrate tetrahydrate in 8.0 mL of 2 M NaOH and 20 mL of 96 mM of 3,5-dinitrosalicylic acid solution) and was boiled for 10 min in a water bath at 85–90 °C. The mixture was cooled to ambient temperature and was diluted with 5 ml of distilled water, and the absorbance was measured at 540 nm using a UV-Visible spectrophotometer. The blank with 100% enzyme activity was prepared by replacing the plant extract with 200 μl of buffer. A blank reaction was similarly prepared using the plant extract at each concentration in the absence of the enzyme solution. A positive control sample was prepared using Acarbose (100 μg/ml–2 μg/ml) and the reaction was performed similarly to the reaction with plant extract as mentioned above. The α-amylase inhibitory activity was expressed as percent inhibition and was calculated using the equation given below: The % α-amylase inhibition was plotted against the extract concentration and the IC50values were obtained from the graph. %αamylaseinhibition=100×Abs100%control−AbsSampleAbs100%Control
Wickramaratne M.N., Punchihewa J.C, & Wickramaratne D.B. (2016). In-vitro alpha amylase inhibitory activity of the leaf extracts of Adenanthera pavonina. BMC Complementary and Alternative Medicine, 16, 466.
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Publication 2016
Acarbose Acids Amylase Bath Biological Assay Buffers enzyme activity Enzymes Exhaling Plant Extracts Plant Leaves Psychological Inhibition Sodium Chloride sodium potassium tartrate Starch Sulfoxide, Dimethyl
2
DILIN Prospective Study of Drug-Induced Liver Injury
Cited 16 times
Patients with suspected DILI were enrolled in the DILIN Prospective Study and data were collected as previously described (5 (link)). Patients or their next of kin provided written informed consent which included pathology review. If available, up to 10 unstained re-cuts of liver tissue (needle or wedge biopsies, explanted native livers and autopsies) obtained at investigator discretion were sent to the central pathology core laboratory (NCI) for repeat staining and storage. Slides were stained with hematoxylin and eosin, Masson trichrome, reticulin, iron, copper and periodic acid-Schiff (PAS) with diastase. Biopsies were reviewed by the central hepatic pathologist (DEK) who was blinded to all clinical information including the name(s) of the implicated drugs. All liver tissues received the same predefined structured histological evaluation. This systematic evaluation of 48 separate histologic features was divided into seven broad categories: inflammation, necrosis/cell injury, fibrosis, steatosis, cholestasis, vascular injury, and other findings including evaluation of special stains (Supplementary Table 1)(10 ). The number of portal areas (complete and partial) was recorded as a measure of biopsy adequacy. The diagnostic classification used (Supplementary Table 2) was based on published descriptions of pathologic changes in DILI (11 , 12 ). Standard hepatopathological diagnostic criteria (13 ) were used to define patterns of injury. The overall injury pattern was classified into one of 18 patterns: acute hepatitis, chronic hepatitis, acute cholestasis, chronic cholestasis, cholestatic hepatitis (mixed hepatocellular and cholestatic injury), granulomatous changes, steatosis (macrovesicular or microvesicular), steatohepatitis, coagulative/confluent necrosis (zonal or non-zonal), massive/sub-massive necrosis, vascular injury, hepatocellular alteration, nodular regenerative hyperplasia, mixed or otherwise unclassifiable injury, minimal non-specific changes, and absolutely normal.
For the purposes of the current analysis, a biopsy was eligible for inclusion if it was obtained within six months of the protocol-defined DILI onset date and was adequate in the pathologist’s opinion to assign a pattern of injury. Tissues from explants or autopsies were excluded. If two biopsies qualified from the same patient, the larger biopsy was used. Once the biopsy data from blinded review was recorded, additional information was abstracted from the DILIN prospective database including the patient age, sex and laboratory data (alanine aminotransferase (ALT), alkaline phosphatase (Alk P) and total bilirubin) at the time of DILI onset and at or around the time of liver biopsy (within 7 days). The biochemical injury pattern (hepatocellular, mixed or cholestatic) was calculated as the ratio (R) of ALT to Alk P normalized by their respective upper limits of normal from laboratory data at the time of onset. If a suspected case had undergone causality determination (9 (link)) then the causality score, severity score and implicated medications were also obtained from the database.
Kleiner D.E., Chalasani N.P., Lee W.M., Fontana R.J., Bonkovsky H.L., Watkins P.B., Hayashi P.H., Davern T.J., Navarro V., Reddy R., Talwalkar J.A., Stolz A., Gu J., Barnhart H, & Hoofnagle J.H. (2013). Hepatic Histological Findings in Suspected Drug-Induced Liver Injury: Systematic Evaluation and Clinical Associations. Hepatology (Baltimore, Md.), 59(2), 661-670.
Publication 2013
Alkaline Phosphatase Amylase Autopsy Bilirubin Biopsy Cell-Derived Microparticles Cells Cholestasis Coagulation, Blood Copper D-Alanine Transaminase Diagnosis Dilin Eosin Fibrosis Granuloma Hepatitis Hepatitis, Chronic Hyperplasia Inflammation Injuries Iron Liver Necrosis Needles Pathologists Patients Periodic Acid Pharmaceutical Preparations Regeneration Reticulin Stains Steatohepatitis Tissues Vascular System Injuries Zonal
3
Screening for α-Amylase Inhibitors in Plants
Cited 16 times
Screening of plant material for α-amylase inhibitors was carried out in a microtitre plate according to Xiao et al (2006) based on the starch-iodine test [23 (link)]. The total assay mixture composed of 40 μl 0.02 M sodium phosphate buffer (pH 6.9 containing 6 mM sodium chloride), 0.02 units of PPA solution and plant extracts at concentration from 0.1-1.5 mgml-1 (w/v) were incubated at 37°C for 10 min. Then soluble starch (1%, w/v) was added to each reaction well and incubated at 37°C for 15 min. 1 M HCl (20 μl) was added to stop the enzymatic reaction, followed by the addition of 100 μl of iodine reagent (5 mM I2 and 5 mM KI). The colour change was noted and the absorbance was read at 620 nm on a microplate reader. The control reaction representing 100% enzyme activity did not contain any plant extract. To eliminate the absorbance produced by plant extract, appropriate extract controls without the enzyme were also included. The known PPA inhibitor, acarbose, was used a positive control at a concentration range of 6.5 - 32.8 μgml-1. A dark-blue colour indicates the presence of starch; a yellow colour indicates the absence of starch while a brownish colour indicates partially degraded starch in the reaction mixture. In the presence of inhibitors from the extracts the starch added to the enzyme assay mixture is not degraded and gives a dark-blue colour complex whereas no colour complex is developed in the absence of the inhibitor, indicating that starch is completely hydrolysed by α-amylase.
P S., Zinjarde S.S., Bhargava S.Y, & Kumar A.R. (2011). Potent α-amylase inhibitory activity of Indian Ayurvedic medicinal plants. BMC Complementary and Alternative Medicine, 11, 5.
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Publication 2011
A-A-1 antibiotic Acarbose Amylase Biological Assay Buffers enzyme activity Enzyme Assays Enzymes inhibitors Plant Extracts Plants Sodium Chloride sodium phosphate Starch
4
Comprehensive Analysis of Ginseng Metabolites
Cited 13 times
Starch was measured via an enzyme hydrolysis method. Starch was hydrolyzed into dual sugars by amylase, hydrolyzed into monosaccharides by hydrochloric acid, and finally determined by reducing sugar, which is converted to starch (Rose et al., 1991 (link)).
The contents of pyruvate in the sample were determined according to the methods of Lin et al. (1995 ). Protein was removed from the samples by TCA precipitation, and in the resulting sample, pyruvate reacted with 2,4-nitrophenylhydrazine. The product turned red in the presence of an alkali solution, and the intensity of the color change was measured by a spectrophotometer. A standard curve for calibration was obtained using sodium pyruvate as a reagent with a gradient of concentrations of pyruvic acid. Absorbance values were obtained to generate a standard curve to calculate the pyruvate concentration.
For glutathione (GSH), roots were ground in liquid nitrogen and homogenized in 1 mL 5% (w/v) m-phosphoric acid containing 1 mM diethylene triamine pentaacetic acid (DTPA) and 6.7% (w/v) sulfosalicylic acid. Root extracts were centrifuged at 12,000 × g for 15 min at 4°C. GSH contents were determined according to the methods of Kortt and Liu (1973 (link)) and Ellman (1959 (link)) with some modifications.
The ascorbic acid (AsA) content was determined according to Egea et al. (2007 (link)) with slight modifications. Ginseng roots were ground in an ice bath with 10 mL 5% metaphosphoric acid stored at 4°C, and then the final mix was homogenized by vortex. The final solution was maintained on the ice bath, in darkness, for 30 min and then centrifuged at 20,000 × g for 25 min at 4°C. Ascorbate was spectrophotometrically detected by measuring absorbance at 254 nm with a UV detector. For quantification of the compound, a calibration curve in the range of 10–100 mg kg−1 was prepared from standard ascorbic acid. Results were expressed as mg 100 g−1 FW.
Root extracts were centrifuged at 12,000 × g for 15 min at 4°C. The extraction and determination of ginsenosides was performed following the method of Yu et al. (2002 (link)).
Ma R., Sun L., Chen X., Mei B., Chang G., Wang M, & Zhao D. (2016). Proteomic Analyses Provide Novel Insights into Plant Growth and Ginsenoside Biosynthesis in Forest Cultivated Panax ginseng (F. Ginseng). Frontiers in Plant Science, 7, 1.
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Publication 2016
4-nitrophenylhydrazine Alkalies Amylase Ascorbic Acid Bath Carbohydrates Darkness Enzymes Ginseng Ginsenosides Hydrochloric acid Hydrolysis metaphosphoric acid Monosaccharides Nitrogen Pentetic Acid Phosphoric Acids Plant Roots Proteins Pyruvates Pyruvic Acid Sodium Starch Sugars sulfosalicylic acid
5
α-Amylase Inhibitory Activity Assay
Cited 13 times
α-amylase inhibitory activity of extract and fractions was carried out according to the standard method with minor modification.[11 (link)] In a 96-well plate, reaction mixture containing 50 μl phosphate buffer (100 mM, pH = 6.8), 10 μl α–amylase (2 U/ml), and 20 μl of varying concentrations of extract and fractions (0.1, 0.2, 0.3, 0.4, and 0.5 mg/ml) was preincubated at 37°C for 20 min. Then, the 20 μl of 1% soluble starch (100 mM phosphate buffer pH 6.8) was added as a substrate and incubated further at 37°C for 30 min; 100 μl of the DNS color reagent was then added and boiled for 10 min. The absorbance of the resulting mixture was measured at 540 nm using Multiplate Reader (Multiska thermo scientific, version 1.00.40). Acarbose at various concentrations (0.1–0.5 mg/ml) was used as a standard. Without test (extract and fractions) substance was set up in parallel as control and each experiment was performed in triplicates. The results were expressed as percentage inhibition, which was calculated using the formula,
Inhibitory activity (%) = (1 − As/Ac) ×100
Where,
As is the absorbance in the presence of test substance and Ac is the absorbance of control.
Telagari M, & Hullatti K. (2015). In-vitro α-amylase and α-glucosidase inhibitory activity of Adiantum caudatum Linn. and Celosia argentea Linn. extracts and fractions. Indian Journal of Pharmacology, 47(4), 425-429.
Publication 2015
Acarbose Amylase Buffers Phosphates Psychological Inhibition Starch

Most recents protocols related to «Amylase»

1
Sensory Evaluation of Glucosyl Stevia Cookies
Not available on PMC !

EXAMPLE 8

Diet Cookies

Flour (50.0%), margarine (30.0%) fructose (10.0%), maltitol (8.0%), whole milk (1.0%), salt (0.2%), baking powder (0.15%), vanillin (0.1%) and different glucosyl Stevia compositions (0.03%) were kneaded well in dough-mixing machine. The obtained dough was molded and baked in oven at 200° C. for 15 minutes. Glucosyl Stevia compositions were by represented by Samples 1a, 2a, and 3, obtained according to EXAMPLES 3, 4, and 5, respectively; with Sample 4 being a commercial β-amylase treated product (containing only mono- and di-α-1,4-glucosyl-derivatives of steviol glycosides).

The sensory properties were evaluated by 20 panelists. The best results were obtained in samples prepared by high purity short-chain glucosyl Stevia compositions (containing four or less α-1,4-glucosyl residues) derivatives (Samples 1a and 2a). The panelists noted rounded and complete flavor profile and mouthfeel in cookies prepared with Samples 1a and 2a.

US11871771B2. Glucosyl Stevia composition (2024-01-16). PureCircle Sdn Bhd [MY]. Inventors: Avetik Markosyan [AM].
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Patent 2024
Amylase baking powder derivatives Flavor Enhancers Flour Fructose maltitol Margarine Milk, Cow's Sodium Chloride Stevia stevioside Therapy, Diet vanillin
2
Inactivation of Rghr2 Regulated Genes
Not available on PMC !

Example 4

Inactivation of Rghr2 Regulated Genes and Their Effect on Heterologous Protein Production

The Bli03644, abrB1, yvzC and abh genes were inactivated by insertion of antibiotic marker in a Bra7 strain producing a heterologous α-amylase (i.e., the heterologous P. curdlanolyticus α-amylase disclosed in PCT Publication No. WO2014/164834), wherein the heterologous α-amylase production was determined in the four single knock-out strains (ΔBLi03644, ΔabrB1, ΔyvzC and Δabh) and compared to the parental (control) strain as described in Example 2. For example, as presented in FIG. 7, inactivation of Bli03644, abrB1, yvzC and abh resulted in improved heterologous α-amylase production, while cell growth (OD600) was less affected.

US11866713B2. Compositions and methods for increased protein production in bacillus licheniformis (2024-01-09). DANISCO US INC [US]. Inventors: Marc Anton Bernhard Kolkman [NL], Steven D. Doig [US], Ryan L. Frisch [US], Hongxian He [US], Frank Wouter Koopman [NL], Chris Leeflang [NL].
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Patent 2024
Amylase Antibiotics Bacillus licheniformis Cells Genes Gene Silencing Parent Proteins Strains
3
Lipase Activity on Omega-3 and Omega-6 Triglycerides
Not available on PMC !

EXAMPLE 10

Rhizopus oryzae (RO) lipase displayed far greater activity toward DHA and ARA triglycerides than porcine pancreatin (Zenpep®), which contains a mixture of pancreatic lipases, proteases, and amylases. 1.4 mL of infant formula was mixed with 100 uL of lipase (either pancreatin or RO lipase) and 100 uL each of triglycerides of DHA and ARA. Reactions were incubated at 37° C. for 15 minutes. Samples were taken at time points 0, 1, 2, 4, 6, 8, 10, and 15 minutes and analyzed by RP-HPLC for DHA and ARA. DHA (FIG. 28A) and ARA (FIG. 28B) triglycerides were hydrolyzed by RO lipase over time but were not hydrolyzed by pancreatin.

US11872191B2. Methods, compositions, and devices for supplying dietary fatty acid needs (2024-01-16). Alcresta Therapeutics, Inc. [US]. Inventors: Alexey L. Margolin [US], Robert Gallotto [US], Bhami Shenoy [US].
Full text: Click here
Patent 2024
Amylase Endopeptidases High-Performance Liquid Chromatographies Infant Formula Lipase Pancreas Pancreatin Pigs Rhizopus oryzae Triglycerides
4
Glucosyl Stevia Yoghurt Formulation
Not available on PMC !

EXAMPLE 9

Yoghurt

Different glucosyl Stevia compositions (0.03%) and sucrose (4%) were dissolved in low fat milk. Glucosyl Stevia compositions were by represented by Samples 1a, 2a, and 3, obtained according to EXAMPLES 3, 4, and 5, respectively; with Sample 4 being a commercial β-amylase treated product (containing only mono- and di-α-1,4-glucosyl-derivatives of steviol glycosides). After pasteurizing at 82° C. for 20 minutes, the milk was cooled to 37° C. A starter culture (3%) was added and the mixture was incubated at 37° C. for 6 hours then at 5° C. for 12 hours.

The sensory properties were evaluated by 20 panelists. The best results were obtained in samples prepared by high purity short-chain glucosyl Stevia compositions (containing four or less α-1,4-glucosyl residues) derivatives (Samples 1a and 2a). The panelists noted rounded and complete flavor profile and mouthfeel in samples prepared with Samples 1a and 2a.

US11871771B2. Glucosyl Stevia composition (2024-01-16). PureCircle Sdn Bhd [MY]. Inventors: Avetik Markosyan [AM].
Full text: Click here
Patent 2024
Amylase derivatives Fat-Restricted Diet Flavor Enhancers Milk Stevia stevioside Sucrose Yogurt
5
Protein Characterization Using Antibodies
Chromatin immunoprecipitation (ChIP), immunoblotting, immunofluorescence, or immunohistochemistry were performed using the following antibodies: anti-α-SMA (#19245T; Cell Signaling); anti-β-Actin (#64225332; Bio-Rad), anti-amylase (#ab21156; Abcam), anti-chromogranin-A (#ab45179; Abcam), anti-cytokeratin 19 (#ab52625; Abcam), anti-E-cadherin (#3195S; Cell Signaling), anti-glucagon (#2760; Cell Signaling), anti-insulin (#4590; Cell Signaling), anti-JunB (#3753; Cell Signaling), anti-Muc5AC (#ab3649; Abcam), anti-Prdm16 (#ab202344 and #ab106410; Abcam), anti-Smad2 (#5339; Cell Signaling), anti-Smad3, (#9523; Cell Signaling), anti-Smad4, (#46535; Cell Signaling), anti-Smad4 (#sc-7966; Santa Cruz), anti-Smad2/3 (#8685; Cell Signaling), and anti-vimentin (#5741S; Cell Signaling).
Hurwitz E., Parajuli P., Ozkan S., Prunier C., Nguyen T.L., Campbell D., Friend C., Bryan A.A., Lu T.X., Smith S.C., Razzaque M.S., Xu K, & Atfi A. (2023). Antagonism between Prdm16 and Smad4 specifies the trajectory and progression of pancreatic cancer. The Journal of Cell Biology, 222(4), e202203036.
Full text: Click here
Publication 2023
Actins Amylase Antibodies Cadherins Chromogranin A Glucagon Immunofluorescence Immunohistochemistry Immunoprecipitation, Chromatin Insulin Keratin-19 MEL1S protein, human MUC5AC protein, human SMAD2 protein, human SMAD3 protein, human SMAD4 protein, human Vimentin

Top products related to «Amylase»

1
α amylase by Merck Group
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α-amylase is an enzyme commonly used in laboratory settings. It functions by catalyzing the hydrolysis of starch, glycogen, and related polysaccharides into smaller carbohydrate units such as maltose and glucose.
2
Pepsin by Merck Group
Sourced in United States, Germany, China, United Kingdom, Italy, Poland, France, Sao Tome and Principe, Spain, Canada, India, Australia, Ireland, Switzerland, Sweden, Japan, Macao, Israel, Singapore, Denmark, Argentina, Belgium
Pepsin is a proteolytic enzyme produced by the chief cells in the stomach lining. It functions to break down proteins into smaller peptides during the digestive process.
3
Acarbose by Merck Group
Sourced in United States, Germany, India, China, Italy, France, Australia, Singapore, United Kingdom, Spain, Brazil
Acarbose is a prescription medication used to help manage blood sugar levels in individuals with diabetes. It works by slowing the breakdown and absorption of carbohydrates in the digestive system, which can help control postprandial (after-meal) blood glucose levels. Acarbose is an enzyme inhibitor that targets alpha-glucosidase, an enzyme responsible for breaking down complex carbohydrates.
4
α glucosidase by Merck Group
Sourced in United States, Germany, China, Italy, Spain, France, United Kingdom, Australia, Macao, Poland
α-glucosidase is an enzyme that catalyzes the hydrolysis of α-1,4-glucosidic linkages in oligosaccharides and disaccharides. It is commonly used in laboratory settings for various analytical and research applications.
5
Gallic acid by Merck Group
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Gallic acid is a naturally occurring organic compound that can be used as a laboratory reagent. It is a white to light tan crystalline solid with the chemical formula C6H2(OH)3COOH. Gallic acid is commonly used in various analytical and research applications.
6
Pancreatin by Merck Group
Sourced in United States, Germany, United Kingdom, Poland, China, Italy, France, Spain, Switzerland, Canada, Australia, India, Ireland, Jersey, Belgium, Sao Tome and Principe, Denmark
Pancreatin is a digestive enzyme complex derived from the pancreas of mammals. It contains a mixture of digestive enzymes, including amylase, lipase, and protease, which play a role in the breakdown of carbohydrates, fats, and proteins, respectively.
7
2 2 diphenyl 1 picrylhydrazyl (dpph) by Merck Group
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DPPH is a chemical compound used as a free radical scavenger in various analytical techniques. It is commonly used to assess the antioxidant activity of substances. The core function of DPPH is to serve as a stable free radical that can be reduced, resulting in a color change that can be measured spectrophotometrically.
8
Quercetin by Merck Group
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Quercetin is a natural compound found in various plants, including fruits and vegetables. It is a type of flavonoid with antioxidant properties. Quercetin is often used as a reference standard in analytical procedures and research applications.
9
Amyloglucosidase by Merck Group
Sourced in United States, Germany, China, Ireland, Japan, United Kingdom, Switzerland, Sao Tome and Principe, Australia, India
Amyloglucosidase is an enzyme that hydrolyzes starch and glycogen to glucose. It is commonly used in the food and beverage industry for the production of glucose syrups and other sweeteners.
10
Bovine serum albumin (bsa) by Merck Group
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.

More about "Amylase"

Amylase, a critical enzyme in carbohydrate metabolism, plays a vital role in the breakdown of starch and glycogen.
This versatile enzyme, found in various organisms including humans, animals, plants, and microorganisms, catalyzes the hydrolysis of alpha-1,4-glucosidic bonds, converting complex polysaccharides into simpler sugars.
Amylase's importance extends beyond its digestive functions, as it is also essential for energy production.
Researchers studying this enzyme can leverage PubCompare.ai's AI-driven platform to effortlessly locate the best protocols from literature, preprints, and patents, ensuring reproducibility and accuracy in their amylase research.
The power of data-driven comparisons offered by PubCompare.ai can enhance research outcomes and advance our understanding of this important enzyme.
Researchers can explore the intricacies of amylase, including its relationship with other key enzymes like α-amylase, Pepsin, Acarbose, α-glucosidase, Gallic acid, Pancreatin, DPPH, Quercetin, and Amyloglucosidase.
By utilizing PubCompare.ai's comprehensive resources, researchers can optimize their amylase studies, leading to groundbreaking discoveries and a deeper comprehension of this vital component of carbohydrate metabolism.
With the ability to easily access the best protocols and leverage data-driven comparisons, researchers can ensure the reproducibility and accuracy of their amylase-related experiments, ultimately advancing our understanding of this critical enzyme.