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Chapter 1: Theory of endo-1, 4-Beta-D-Xylanase Assay Procedure
Chapter 2: Buffers & Reagents
Chapter 3: Assay Procedure
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|Stability:||> 10 years under recommended storage conditions|
|Substrate For (Enzyme):||α-amylase|
|Reproducibility (%):||~ 5%|
High purity dyed and crosslinked Amylazyme tablets for the measurement of diastase activity (α-amylase) in honey.
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 HY Tablets is equivalent to this.
K-AMYLSD - α-Amylase SD Assay Kit R-CAAR4 - α-Amylase Reagent (Ceralpha) R-AMHR4 - α-Amylase HR Reagent T-AMZ-200T - Amylazyme Tablets T-AMZBG-200T - Amylazyme BG Tablets T-AMZRD-200T - Amylazyme Red Tablets S-RSTAR - Red Starch I-AZAMY - AZCL-Amylose I-AZAMYF - AZCL-Amylose (fine) I-RCLAMYF - RedCL-Amylose (fine) K-MALTA - Malt Amylase Assay Kit
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.Hide Abstract
Molecular characterization of Maltese honey: diastase and proline levels changes in Maltese honey seasons.
Douglas, A. B., Attard, E. & Camilleri, C. (2013). Farm Animal Proteomics, 266-269.
A research project between the Division of Rural Sciences and Food Systems at the University of Malta and Golden Island Ltd. Is currently analysing in detail the physicochemical characteristics of Maltese Honey following internationally recognized standard techniques. Among the parameters being analysed are the amino acid proline and the enzyme diastase.Hide Abstract
Direct potentiometric determination of diastase activity in honey.
Sak-Bosnar, M. & Sakač, N. (2012). <i>Food Chemistry</i>, 135(2), 827-831.
A novel method for the determination of diastase activity is reported. The method is based on a direct potentiometric measurement of triiodide ion that is released when a starch–triiodide complex is hydrolysed by honey diastase. The increase of free triiodide ion concentration in a sample is found to be directly proportional to the diastase activity of the sample. A response mechanism of the platinum redox electrode is proposed, allowing a calculation of the diastase activity factor (<i>F</i>). The sensor and analyte parameters, including <i>F</i>, were obtained by least squares fitting of potentiometric data using the optimisation function of the Solver add-in of Microsoft Excel. The values of <i>F</i> obtained by the new direct potentiometric method were compared with those obtained using the standard Phadebas method (DN values), and the two values were found to agree within experimental error. Finally, the diastase activity of nine varieties of honey was determined using the novel method developed here.Hide Abstract