Amylazyme Tablets

Play Training Video
Analysis of enzymes activity using carbohydrase tablet testing

To choose a chapter, play the video and select the required chapter from the options on the video display.

Chapter 1: Theory of endo-1, 4-Beta-D-Xylanase Assay Procedure
Chapter 2: Buffers & Reagents
Chapter 3: Assay Procedure
 
Reference code: T-AMZ-200T
SKU: 700005094

Content:

200 Tablets

Content: 200 Tablets or 1,000 Tablets
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Solid
Stability: > 2 years under recommended storage conditions
Substrate For (Enzyme): α-amylase
Assay Format: Spectrophotometer
Detection Method: Absorbance
Wavelength (nm): 590
Reproducibility (%): ~ 5%
Method recognition: AACC Method 22-05.01 and RACI Standard Method

High purity dyed and crosslinked Amylazyme tablets for the measurement of enzyme activity, for research, biochemical enzyme assays and in vitro diagnostic analysis.

For the assay of cereal and microbial α-amylase. Containing AZCL-Amylose. Recommended substrate for the assay of α-amylase in weather-damaged cereal grains, honey samples and food products containing low levels of this activity.

Please note the video above shows the protocol for assay of endo-xylanase using xylazyme tablets. The procedure for the assay of α-amylase using Amylazyme Tablets is equivalent to this.

Browse more of our enzyme tablet tests.

Validation of Methods

  

Documents
Certificate of Analysis
Safety Data Sheet
FAQs Application Note Assay Protocol
Publications
Megazyme publication

Measurement of α-Amylase in Cereal, Food and Fermentation Products.

McCleary, B. V. & Sturgeon, R. (2002). Cereal Foods World, 47, 299-310.

In General, the development of methods for measuring α-amylase is pioneered in the clinical chemistry field and then translated to other industries, such as the cereals and fermentation industries. In many instances, this transfer of technology has been difficult or impossible to achieve due to the presence of interfering enzymes or sugars and to differences in the properties of the enzymes being analysed. This article describes many of the commonly used methods for measuring α-amylase in the cereals, food, and fermentation industries and discusses some of the advantages and limitations of each.

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Megazyme publication

Optimising the response.

Acamovic, T. & McCleary, B. V. (1996). Feed Mix, 4, 14-19.

A fine balance exists between enzyme activity and the adverse effects associated with feed processing. Accurate estimation of enzyme activity in the feed is a pre-requisite to optimising the response.

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Megazyme publication
Comparison of endolytic hydrolases that depolymerise 1,4-β-D-mannan, 1,5-α-L-arabinan and 1,4-β-D-galactan.

McCleary, B. V. (1991). “Enzymes in Biomass Conversion”, (M. E. Himmel and G. F. Leatham, Eds.), ACS Symposium Series, 460, Chapter 34, pp. 437-449. American Chemical Society, Washington.

Hydrolysis of mannan-type polysaccharides by β-mannanase is dependent on substitution on and within the main-chain as well as the source of the β-mannanase employed. Characterisation of reaction products can be used to define the sub-site binding requirements of the enzymes as well as the fine-structures of the polysaccharides. Action of endo-arabinanase and endo-galactanase on arabinans and arabinogalactans is described. Specific assays for endo-arabinanase and arabinan (in fruit-juice concentrates) are reported.

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Megazyme publication

Measurement of polysaccharide degrading enzymes using chromogenic and colorimetric substrates.

McCleary, B. V. (1991). Chemistry in Australia, September, 398-401.

Enzymic degradation of carbohydrates is of major significance in the industrial processing of cereals and fruits. In the production of beer, barley is germinated under well defined conditions (malting) to induce maximum enzyme synthesis with minimum respiration of reserve carbohydrates. The grains are dried and then extracted with water under controlled conditions. The amylolytic enzymes synthesized during malting, as well as those present in the original barley, convert the starch reserves to fermentable sugars. Other enzymes act on the cell wall polysaccharides, mixed-linkage β-glucan and arabinoxylan, reducing the viscosity and thus aiding filtration, and reducing the possibility of subsequent precipitation of polymeric material. In baking, β-amylase and α-amylase give controlled degradation of starch to fermentable sugars so as to sustain yeast growth and gas production. Excess quantities of α-amylase in the flour result in excessive degradation of starch during baking which in turn gives a sticky crumb texture and subsequent problems with bread slicing. Juice yield from fruit pulp is significantly improved if cell-wall degrading enzymes are used to destroy the three-dimensional structure and water binding capacity of the pectic polysaccharide components of the cell walls. Problems of routine and reliable assay of carbohydrate degrading enzymes in the presence of high levels of sugar compounds are experienced with such industrial process.

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Megazyme publication
New chromogenic substrates for the assay of alpha-amylase and (1→4)-β-D-glucanase.

McCleary, B. V. (1980). Carbohydrate Research, 86(1), 97-104.

New chromogenic substrates have been developed for the quantitative assay of alpha-amylase and (1→4)-β-D-glucanase. These were prepared by chemically modifying amylose or cellulose before dyeing, to increase solubility. After dyeing, the substrates were either soluble or could be readily dispersed to form fine, gelatinous suspensions. Assays based on the use of these substrates are sensitive and highly specific for either alpha-amylase or (1→4)-β-D-glucanase. The method of preparation can also be applied to obtain substrates for other endo-hydrolases.

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Publication

The effect of sprouted wheat wholemeal inclusion in bread recipes on postprandial blood glucose and satiety responses in healthy adults: a randomized trial.

Cao, W., Tucker, A., Hoang, A., Abdi, R., Wright, A. & Joye, I. J. (2024). Journal of Functional Foods, 121, 106447.

Sprouted wheat wholemeal was reported to enhance the nutritional and sensory properties of cereal products, but few human studies exist. The effect of blending 50 % sprouted wheat wholemeal in a bread recipe on the postprandial glycemic and satiety responses, and sensory-related sensations was investigated in this randomized crossover human study with 12 healthy participants. Capillary blood samples were collected and glycemic response was determined at 0, 15, 30, 45, 60, 90, 120 min. Satiety visual analogue scales were given every 30 min. While substituting bread wheat flour with sprouted wheat wholemeal significantly increased the α-amylase activity in the dough (p < 0.05), it did not alter in vitro digestibility or postprandial glycemic and satiety responses (p > 0.05). Likewise, participant overall acceptability was not adversely affected. Sprouted wheat wholemeal can be used as a functional ingredient in breadmaking, although it did not, in this study, significantly affect digestibility parameters.

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Publication

A study to clarify whether sunn pest (Eurygaster integriceps) increases amylase activity in wheat.

Dizlek, H. & Özer, M. S. (2024). Heliyon, 10(10).

There is uncertainty as to whether amylase is injected into wheat kernels by the sunn pest (SP). There are conflicting results in the literature as to whether the amylolytic activity (AA) of insect-damaged wheat is increased. Therefore, the research question of this study is whether amylase is injected into wheat kernels by SP. Two bread wheat cultivars with different levels of SP-damage were used (first year Golia 2.35% SP damaged kernel ratio [SPDR], second year Golia 3.92% SPDR and Sagittario 7.8% SPDR). Sound and SP-damaged wheat (SPDW) kernels were manually separated. In addition, SPDW kernels were divided into four categories according to their infection rates. The AA of these different wheats was determined by using AACC methods 22-05.01 and 56–81.04. In cultivar Golia, the α-amylase activity of the most damaged wheat (C4/4 WGWF) was 9.5 times higher than that of the undamaged wheat. The SP-damaged samples had a lower Falling Number (FN), i.e. higher AA, than the undamaged samples in both cultivars. The FN values of the flour samples prepared from the 100% SPDW were reduced by up to 40% compared to the undamaged samples. In conclusion, we clearly found increased amylase activity in SPDW. As the proportion of insect-damaged kernels in the wheat mass increased, the AA of the wheat and its flour also increased, as did the proteolytic activity. Because the AA in some wheats is insufficient for bread-making, SPDW can be blended to sound wheat varieties within certain limits to reduce or reset the use of amylase base additives and reduce bread costs.

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Publication

The High Pressure Preservation of Honey: A Comparative Study on Quality Changes during Storage.

Scepankova, H., Majtan, J., Estevinho, L. M. & Saraiva, J. A. (2024). Foods, 13(7), 989.

In commercially available honey, the application of a heat treatment to prevent spoilage can potentially compromise its beneficial properties and quality, and these effects worsen with extended storage. The high-pressure processing (HPP) of honey is being explored, but its long-term impact on honey quality has not been characterised yet. This study evaluated the effects of HPP and thermal processing on the microbial load, physicochemical quality (i.e., hydroxymethylfurfural content and diastase activity), and antioxidant capacity of honey after treatment and following extended storage (6, 12, and 24 months) at 20°C. Pasteurization (78°C/6 min) effectively eliminated the microorganisms in honey but compromised its physicochemical quality and antioxidant activity. HPP initially showed sublethal inactivation, but storage accelerated the decrease in yeasts/moulds and aerobic mesophiles in honey (being <1 log CFU/g after 24 months of storage) compared to unprocessed honey and honey thermally treated under mild conditions (55°C/15 min). The physicochemical characteristics of the quality of HPP-treated honey and raw unprocessed honey did change after long-term storage (24 months) but remained within regulatory standards. In conclusion, HPP emerged as a more suitable and safe preservation method for Apis mellifera honey, with a minimal risk of a loss of antioxidant activity compared to traditional industrial honey pasteurization.

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Publication

The role of α-glucosidase in germinating barley grains.

Stanley, D., Rejzek, M., Naested, H., Smedley, M., Otero, S., Fahy, B., et al.. (2011). Plant Physiology, 155(2), 932-943.

The importance of α-glucosidase in the endosperm starch metabolism of barley (Hordeum vulgare) seedlings is poorly understood. The enzyme converts maltose to glucose (Glc), but in vitro studies indicate that it can also attack starch granules. To discover its role in vivo, we took complementary chemical-genetic and reverse-genetic approaches. We identified iminosugar inhibitors of a recombinant form of an α-glucosidase previously discovered in barley endosperm (ALPHA-GLUCOSIDASE97 [HvAGL97]), and applied four of them to germinating grains. All four decreased the Glc-to-maltose ratio in the endosperm 10 d after imbibition, implying inhibition of maltase activity. Three of the four inhibitors also reduced starch degradation and seedling growth, but the fourth did not affect these parameters. Inhibition of starch degradation was apparently not due to inhibition of amylases. Inhibition of seedling growth was primarily a direct effect of the inhibitors on roots and coleoptiles rather than an indirect effect of the inhibition of endosperm metabolism. It may reflect inhibition of glycoprotein-processing glucosidases in these organs. In transgenic seedlings carrying an RNA interference silencing cassette for HvAgl97, α-glucosidase activity was reduced by up to 50%. There was a large decrease in the Glc-to-maltose ratio in these lines but no effect on starch degradation or seedling growth. Our results suggest that the α-glucosidase HvAGL97 is the major endosperm enzyme catalyzing the conversion of maltose to Glc but is not required for starch degradation. However, the effects of three glucosidase inhibitors on starch degradation in the endosperm indicate the existence of unidentified glucosidase(s) required for this process.

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Publication

Gibberellins in developing wheat grains and their relationship to late maturity α-amylase (LMA).

Mares, D., Derkx, A., Cheong, J., Zaharia, I., Asenstorfer, R. & Mrva, K. (2022). Planta, 255(6), 1-18.

Late-maturity α-amylase (LMA) in wheat (Triticum aestivum L.) involves the synthesis of α-amylase by the aleurone tissue during grain development. Previous research identified a putative ent-copalyl diphosphate synthase gene, coding for an enzyme that controls the first step in gibberellin biosynthesis, that underlies the major genetic locus involved in variation in LMA phenotype. The reported results for gene transcript analysis, preliminary gibberellin analysis and the effects of DELLA mutants on LMA phenotype appeared to be consistent with involvement of gibberellin but did not provide definitive proof of a causal link. Conversely, several observations do not appear to be consistent with this hypothesis. In this current study, LMA phenotype, gibberellin profiles and ABA content were recorded for experiments involving susceptible and resistant genotypes, gibberellin biosynthesis inhibitors, genetic lines containing different LMA quantitative trait loci and treatment of distal halves of developing grains with exogenous gibberellin. The results suggested that gibberellin may not be a prerequisite for LMA expression and further that the mechanism involved in triggering α-amylase synthesis did not correspond to the model proposed for germination and gibberellin challenged aleurone of ripe grain. The results provide new insight into LMA and highlight the need to investigate alternate pathways for the induction of α-amylase gene transcription, the function of novel 1-β-OH gibberellins and other functions of DELLA proteins in developing grains.

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Safety Data Sheet
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