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1,3-β-Glucazyme Tablets

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Analysis of enzymes activity using carbohydrase tablet testing

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Chapter 1: Theory of endo-1, 4-Beta-D-Xylanase Assay Procedure
Chapter 2: Buffers & Reagents
Chapter 3: Assay Procedure
1-3-beta-Glucazyme Tablets T-PAZ-200T T-PAZ
   
Product code: T-PAZ-200T
€249.00

200 Tablets

Prices exclude VAT

Available for shipping

Content: 200 Tablets
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Solid
Stability: > 10 years under recommended storage conditions
Substrate For (Enzyme): endo-1,3-β-Glucanase
Assay Format: Spectrophotometer
Detection Method: Absorbance
Wavelength (nm): 590
Reproducibility (%): ~ 5%

High purity dyed and crosslinked 1,3-β-Glucazyme tablets for the measurement of enzyme activity, for research, biochemical enzyme assays and in vitro diagnostic analysis.

For the assay of endo-1,3-β-D-glucanase (laminarinase). Containing AZCL-Pachyman; a 1,3-β-D-glucan.

Please note the video above shows the protocol for assay of endo-xylanase using xylazyme tablets. The procedure for the assay of endo-1,3-β-glucanase using 1,3-β-Glucazyme Tablets is equivalent to this.

View more β-Glucazyme tablets and enzyme tablet test products.

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Certificate of Analysis
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Publications
Publication

Characterization and emulsifying properties of extracts obtained by physical and enzymatic methods from an oenological yeast strain.

De Iseppi, A., Curioni, A., Marangon, M., Vincenzi, S., Kantureeva, G. & Lomolino, G. (2019). Journal of the Science of Food and Agriculture, 99(13), 5702-5710.

Background: Glycosylated compounds are one of the main fractions of the yeast cell wall. Thanks to their amphiphilic structure, they have been studied as stabilizers in food emulsions over a broad range of pH conditions with encouraging results. Nevertheless, extraction costs still represent an important limit for their application in the food industry. Results: In this research, four extraction methods were applied to yeast cells exploiting both physical (heating and sonication) and enzymatic approaches (use of three industrial enzyme preparations, namely Glucanex®, Sur Lies and Elevage). A fifth method involving a pure β‐glucanase enzyme (Zymolyase) was taken as reference. These extraction methods were applied to the oenological strain Saccharomyces cerevisiae EC1118, and their extraction yields and chemical properties (quantitative and qualitative determination of sugars and proteins) were studied. Emulsifying activities were determined at three different pH values (3, 5 and 7). Extractions with Physical, Glucanex and Sur Lies methods were the most successful approaches to obtain relevant amounts of yeast compounds with good emulsifying activities for 2:1 oil‐in‐water emulsions at pH 3 and 7 over 48 h. Conclusions: These results indicate that there is the potential for the extraction approaches here proposed to become viable tools for the recovery of yeast compounds to be used as emulsifiers in foods. This approach can be considered as the starting point to explore the possibility to exploit yeast by‐products from the fermentation processes (e.g. fermentation lees from wine and beer making) as valuable compounds for food applications.

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Publication
Lentinula edodes tlg1 encodes a thaumatin-like protein that is involved in lentinan degradation and fruiting body senescence.

Sakamoto, Y., Watanabe, H., Nagai, M., Nakade, K., Takahashi, M. & Sato, T. (2006). Plant Physiology, 141(2), 793-801.

Lentinan is an antitumor product that is purified from fresh Lentinula edodes fruiting bodies. It is a cell wall component, comprising β-1,3-glucan with β-1,6-linked branches, which becomes degraded during postharvest preservation as a result of increased glucanase activity. In this study, we used N-terminal amino acid sequence to isolate tlg1, a gene encoding a thaumatin-like (TL) protein in L. edodes. The cDNA clone was approximately 1.0 kb whereas the genomic sequence was 2.1 kb, and comparison of the two indicated that tlg1 contains 12 introns. The tlg1 gene product (TLG1) was predicted to comprise 240 amino acids, with a molecular mass of 25 kD and isoelectric point value of 3.5. The putative amino acid sequence exhibits approximately 40% identity with plant TL proteins, and a fungal genome database search revealed that these TL proteins are conserved in many fungi including the basidiomycota and ascomycota. Transcription of tlg1 was not detected in vegetative mycelium or young and fresh mushrooms. However, transcription increased following harvest. Western-blot analysis demonstrated a rise in TLG1 levels following harvest and spore diffusion. TLG1 expressed in Escherichia coli and Aspergillus oryzae exhibited β-1,3-glucanase activity and, when purified from the L. edodes fruiting body, demonstrated lentinan degrading activity. Thus, we suggest that TLG1 is involved in lentinan and cell wall degradation during senescence following harvest and spore diffusion.

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Safety Data Sheet
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