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Maltohexaose

Maltopentaose O-MAL6
Product code: O-MAL6
€166.00

250 mg

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Content: 250 mg
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Powder
Stability: > 10 years under recommended storage conditions
CAS Number: 34620-77-4
Molecular Formula: C36H62O31
Molecular Weight: 990.86
Purity: > 90%
Substrate For (Enzyme): Amyloglucosidase, α-amylase, β-Amylase

High purity Maltohexaose for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

Documents
Certificate of Analysis
Safety Data Sheet
Data Sheet
Publications
Publication

The molecular state of gelatinized starch in surplus bread affects bread recycling potential.

Immonen, M., Maina, N. H., Coda, R. & Katina, K. (2021). LWT, 150, 112071.

Surplus bread is a major bakery side stream that should be strictly kept within the human food chain to reduce waste and ensure resource efficiency in baking processes. Optimally, surplus bread should be recycled as a dough ingredient, however, this is known to be detrimental to the volume and texture of bread. The purpose of this study was to investigate how gelatinized starch in surplus bread, untreated or enzymatically hydrolyzed, affects dough development, bread volume and textural attributes. Starch was hydrolyzed to various degrees using commercial α-amylase and amyloglucosidase. Bread hydrolysates containing different carbohydrate profiles (untreated, 75%, 57%, and 26% starch remaining) were evaluated as dough ingredients. More complete starch hydrolysis resulted in better dough visco-elastic properties and higher dough level, and reduced dough water absorption by 13%. Nonetheless, breads containing hydrolysate with high-malto-oligosaccharides had the lowest intrinsic hardness and similar volume yield when compared to control bread. Furthermore, compared to untreated slurry, the hydrolysate with high-malto-oligosaccharides, reduced crumb hardness by 28% and staling rate by 42%, and increased specific volume by 8%. The present findings show that enzymatic hydrolysis dramatically transforms the impact of gelatinized starch. Thus, by selecting correct bioprocessing approaches, bread recycling performance may be significantly improved.

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Publication

Novel cold-adapted raw-starch digesting α-amylases from Eisenia fetida: Gene cloning, expression, and characterization.

Tsukamoto, K., Ariki, S., Nakazawa, M., Sakamoto, T. & Ueda, M. (2021). Biotechnology Reports, 31, e00662.

We identified the raw-starch-digesting α-amylase genes a earthworm Eisenia fetid α amylase I and II (Ef-Amy I and Ef-Amy II). Each gene consists of 1,530 base pairs (bp) that encode proteins of 510 amino acids, as indicated by the corresponding mRNA sequences. Ef-Amy I and II showed an 89% amino acid identity. The amino acid sequences of Ef-Amy I and II were similar to those of the α-amylases from porcine pancreas, human pancreas, Tenebrio molitor, Oryctolagus cuniculus, and Xenopus (Silurana) tropicalis. Each gene encoding mature Ef-Amy I and II was expressed in the GS115 strain of Pichia pastoris. The molecular masses of the recombinant Ef-Amy I and II were 57 kDa each, and catalytically important residues of α-amylases of the GH family 13 were conserved in both proteins. These amylases exhibited raw-starch-digesting activity at 4°C. The substrate specificities of rEf-Amy I and II were dissimilar. rEf-Amy I and II were shown to be active even in 40% ethanol, 4 M NaCl, and 4 M KCl.

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Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
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