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α-Amylase (Aspergillus oryzae)

Product code: E-ANAAM
€187.00

20,000 Units

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Content: 20,000 Units
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In 3.2 M ammonium sulphate
Physical Form: Suspension
Stability: > 1 year under recommended storage conditions
Enzyme Activity: α-Amylase
EC Number: 3.2.1.1
CAZy Family: GH13
CAS Number: 9000-90-2
Synonyms: alpha-amylase; 4-alpha-D-glucan glucanohydrolase
Source: Aspergillus oryzae
Molecular Weight: 54,000
Concentration: Supplied at ~ 1,000 CU/mL
Expression: From Aspergillus oryzae
Specificity: endo-hydrolysis of α-1,4-D-glucosidic linkages in starch.
Specific Activity: ~ 120 U/mg (40oC, pH 5.4 on Ceralpha Reagent)
Unit Definition: One Unit of α-amylase is the amount of enzyme required to release one µmole of p-nitrophenol from blocked p-nitrophenyl-maltoheptaoside per minute (in the presence of excess α-glucosidase), pH 5.4 at 40oC, and is termed a Ceralpha Unit.
Temperature Optima: 50oC
pH Optima: 5
Application examples: For use in Megazyme Starch Damage method.

High purity α-Amylase (Aspergillus oryzae) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

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Documents
Certificate of Analysis
Safety Data Sheet
Data Sheet
Publications
Megazyme publication

Measurement of α-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the ceralpha assay: Collaborative study.

McCleary, B. V., McNally, M., Monaghan, D. & Mugford, D. C. (2002). Journal of AOAC International, 85(5), 1096-1102.

This study was conducted to evaluate the method performance of a rapid procedure for the measurement of α-amylase activity in flours and microbial enzyme preparations. Samples were milled (if necessary) to pass a 0.5 mm sieve and then extracted with a buffer/salt solution, and the extracts were clarified and diluted. Aliquots of diluted extract (containing α-amylase) were incubated with substrate mixture under defined conditions of pH, temperature, and time. The substrate used was nonreducing end-blocked p-nitrophenyl maltoheptaoside (BPNPG7) in the presence of excess quantities of thermostable α-glucosidase. The blocking group in BPNPG7 prevents hydrolysis of this substrate by exo-acting enzymes such as amyloglucosidase, α-glucosidase, and β-amylase. When the substrate is cleaved by endo-acting α-amylase, the nitrophenyl oligosaccharide is immediately and completely hydrolyzed to p-nitrophenol and free glucose by the excess quantities of α-glucosidase present in the substrate mixture. The reaction is terminated, and the phenolate color developed by the addition of an alkaline solution is measured at 400 nm. Amylase activity is expressed in terms of Ceralpha units; 1 unit is defined as the amount of enzyme required to release 1 µmol p-nitrophenyl (in the presence of excess quantities of α-glucosidase) in 1 min at 40°C. In the present study, 15 laboratories analyzed 16 samples as blind duplicates. The analyzed samples were white wheat flour, white wheat flour to which fungal α-amylase had been added, milled malt, and fungal and bacterial enzyme preparations. Repeatability relative standard deviations ranged from 1.4 to 14.4%, and reproducibility relative standard deviations ranged from 5.0 to 16.7%.

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Megazyme publication

New developments in the measurement of α-amylase, endo-protease, β-glucanase and β-xylanase.

McCleary, B. V. & Monaghan, D. (2000). “Proceedings of the Second European Symposium on Enzymes in Grain Processing”, (M. Tenkanen, Ed.), VTT Information Service, pp. 31-38.

Over the past 8 years, we have been actively involved in the development of simple and reliable assay procedures, for the measurement of enzymes of interest to the cereals and related industries. In some instances, different procedures have been developed for the measurement of the same enzyme activity (e.g. α-amylase) in a range of different materials (e.g. malt, cereal grains and fungal preparations). The reasons for different procedures may depend on several factors, such as the need for sensitivity, ease of use, robustness of the substrate mixture, or the possibility for automation. In this presentation, we will present information on our most up-to-date procedures for the measurement of α-amylase, endo-protease, β-glucanase and β-xylanase, with special reference to the use of particular assay formats in particular applications.

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Megazyme publication
An improved enzymic method for the measurement of starch damage in wheat flour.

Gibson, T. S., Al Qalla, H. & McCleary, B. V. (1992). Journal of Cereal Science, 15(1), 15-27.

An improved enzymic method for the determination of starch damage in wheat flour has been developed and characterized. The proposed method is simple and reliable, and enables up to 20 samples to be measured in duplicate in 2 h. A single assay takes approximately 40 min. The assay protocol is in two phases. In the first, the flour sample is incubated with purified fungal alpha-amylase to liberate damaged starch granules as soluble oligosaccharides. After centrifugation, the oligosaccharides in the supernatant are hydrolysed by amyloglucosidase to glucose in phase 2. The glucose is then quantified with a glucose oxidase/peroxidase reagent. The proposed method therefore avoids potential errors associated with existing standard assays, which employ unpurified amylase preparations and non-specific reducing group methods to quantify the hydrolytic products. Despite the use of purified assay components, the proposed starch damage method did not exhibit an absolute end-point to the action of alpha-amylase in phase 1. This was due to a low rate of hydrolysis of undamaged granules, and is a feature of enzymic methods for starch damage determination. Other amylolytic enzymes, including beta-amylase, isoamylase and pullulanase, and combinations of these enzymes, were evaluated as alternatives to alpha-amylase in the proposed method. These enzymes, when used alone, gave no benefits over the use of alpha-amylase. When used in combination with alpha-amylase, there was a synergistic action on undamaged granules. A test kit based on the assay format described in this paper is the subject of an international interlaboratory evaluation.

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Megazyme publication
A new procedure for the measurement of fungal and bacterial α-amylase.

Sheehan, H. & McCleary, B. V. (1988). Biotechnology Techniques, 2(4), 289-292.

A procedure for the measurement of fungal and bacterial α-amylase in crude culture filtrates and commercial enzyme preparations is described. The procedure employs end-blocked (non-reducing end) p-nitrophenyl maltoheptaoside in the presence of amyloglucosidase and α-glucosidase, and is absolutely specific for α-amylase. The assay procedure is simple, reliable and accurate.

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Megazyme publication

Measurement of cereal α-Amylase: A new assay procedure.

McCleary, B. V. & Sheehan, H. (1987). Journal of Cereal Science, 6(3), 237-251.

A new procedure for the assay of cereal α-amylase has been developed. The substrate is a defined maltosaccharide with an α-linked nitrophenyl group at the reducing end of the chain, and a chemical blocking group at the non-reducing end. The substrate is completely resistant to attack by β-amylase, glucoamylase and α-glucosidase and thus forms the basis of a highly specific assay for α-amylase. The reaction mixture is composed of the substrate plus excess quantities of α-glucosidase and glucoamylase. Nitrophenyl-maltosaccharides released on action of α-amylase are instantaneously cleaved to glucose plus free p-nitrophenol by the glucoamylase and α-glucosidase, such that the rate of release of p-nitrophenol directly correlates with α-amylase activity. The assay procedure shows an excellent correlation with the Farrand, the Falling Number and the Phadebas α-amylase assay procedures.

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Publication

Microbial liberation of N-methylserotonin from orange fiber in gnotobiotic mice and humans.

Han, N. D., Cheng, J., Delannoy-Bruno, O., Webber, D., Terrapon, N., Henrissat, B., et al. (2022). Cell, 185(14), 2495-2509.

Plant fibers in byproduct streams produced by non-harsh food processing methods represent biorepositories of diverse, naturally occurring, and physiologically active biomolecules. To demonstrate one approach for their characterization, mass spectrometry of intestinal contents from gnotobiotic mice, plus in vitro studies, revealed liberation of N-methylserotonin from orange fibers by human gut microbiota members including Bacteroides ovatus. Functional genomic analyses of B. ovatus strains grown under permissive and non-permissive N-methylserotonin “mining” conditions revealed polysaccharide utilization loci that target pectins whose expression correlate with strain-specific liberation of this compound. N-methylserotonin, orally administered to germ-free mice, reduced adiposity, altered liver glycogenesis, shortened gut transit time, and changed expression of genes that regulate circadian rhythm in the liver and colon. In human studies, dose-dependent, orange-fiber-specific fecal accumulation of N-methylserotonin positively correlated with levels of microbiome genes encoding enzymes that digest pectic glycans. Identifying this type of microbial mining activity has potential therapeutic implications.

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Publication

Biocatalytic quantification of α‐glucan in marine particulate organic matter.

Steinke, N., Vidal‐Melgosa, S., Schultz‐Johansen, M. & Hehemann, J. H. (2022). MicrobiologyOpen, 11(3), e1289.

α-Glucans can be quantified alongside laminarin in marine particulate organic matter samples using structure-specific hydrolytic enzymes in combination with glucose detection by high-performance anion-exchange chromatography and pulsed amperometric detection. This enzymatic method is a new tool for the characterization and quantification of specific algal glycans in the ocean, which is important to understanding microbial carbon cycling and carbon sequestration in the marine environment.

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Publication

Sink strength of citrus rootstocks under water deficit.

da Silva, S. F., Miranda, M. T., Costa, V. E., Machado, E. C. & Ribeiro, R. V. (2021). Tree Physiology, In Press.

Carbon allocation between source and sink organs determines plant growth and is influenced by environmental conditions. Under water deficit, plant growth is inhibited before photosynthesis and shoot growth tends to be more sensitive than root growth. However, the modulation of source-sink relationship by rootstocks remain unsolved in citrus trees under water deficit. Citrus plants grafted on Rangpur lime are drought tolerant, which may be related to a fine coordination of the source-sink relationship for maintaining root growth. Here, we followed 13C allocation and evaluated physiological responses and growth of Valencia orange trees grafted on three citrus rootstocks (Rangpur lime, Swingle citrumelo and Sunki mandarin) under water deficit. As compared to plants on Swingle and Sunki rootstocks, ones grafted on Rangpur lime showed higher stomatal sensitivity to the initial variation of water availability and less accumulation of non-structural carbohydrates in roots under water deficit. High 13C allocation found in Rangpur lime roots indicates this rootstock has high sink demand associated with high root growth under water deficit. Our data suggest that Rangpur lime rootstock used photoassimilates as sources of energy and carbon skeletons for growing under drought, which is likely related to increases in root respiration. Taken together, our data revealed that carbon supply by leaves and delivery to roots are critical for maintaining root growth and improving drought tolerance, with citrus rootstocks showing differential sink strength under water deficit.

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Publication

Reliability factor for identification of amylolytic enzyme activity in the optimized starch-iodine assay.

Gaenssle, A. L., van der Maarel, M. J. & Jurak, E. (2020). Analytical Biochemistry, 113696.

Amylolytic enzymes are a group of proteins degrading starch to its constitutional units. For high-throughput screening, simple yet accurate methods in addition to the reducing ends assays are required. In this article, the iodine assay, a photometric assay based on the intensely colored starch-iodine complex, was adapted to enable accurate and objective differentiation between enzyme and background activity using a newly introduced mathematical factor. The method was further improved by designing a simple setup for multiple time point detection and discussing the applicability of single wavelength measurements.

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Publication

Stem and leaf functional traits allow successional classification in six pioneer and non-pioneer tree species in Tropical Moist Broadleaved Forests.

Macieira, B. P. B., Locosselli, G. M., Buckeridge, M. S., Hartmann, H. & Cuzzuol, G. R. F. (2020). Ecological Indicators, 113, 106254.

More than half of the tropical forests are secondary forests that are undergoing a highly dynamic interplay of forest succession of uncertain outcome. Vegetation models can help predict forest trajectory but require simplifying the high biodiversity of these forests into a few distinct classes of functional or successional groups. The classification of tree species by successional groups has traditionally relied on qualitative criteria such as life span, or on parameters that are difficult to measure on mature trees in the field, like photosynthetic activity, in particular in tropical forests. Hence, quantitative traits that can be easily measured in a number of species may provide more accurate classification thresholds. The present study identifies quantitative anatomical and biochemical traits of leaf and stem of six species that are useful for classification of successional groups in the Tropical Moist Broadleaved Forest (TMBF) of south-eastern Brazil. Consistent with assumed fast growth and high light requirements of pioneers the investigated pioneer species presented higher stem glucose content (600%), larger vessel elements (162%), greater stomatal density (72%) and higher chloroplastic pigments concentrations (90%) than non-pioneer species. By contrast, non-pioneers were characterized by larger mesophyll cells (70%) and higher cell wall polymers concentrations (65–100%) in leaf and stem. The biggest differences between pioneer and non-pioneer species were observed in leaf blade thickness, followed by vessel lumen diameter, and stem lignin. We provide research laboratories a variety of different tools that they can use as a guideline to accurately assess the successional class of tree species in the TMBF of south-eastern Brazil.

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Safety Information
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Precautionary Statements : Not Applicable
Safety Data Sheet
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