White crystalline powder
D-Glucose, O-α-D-glucopyranosyl-(1->;4)-O-α-D-glucopyranosyl-(1->4)-/α-D-Glucopyranosyl-(1->4)-α-D-glucopyranosyl-(1->4)-D-glucose/O-α-D-Glucopyranosyl-(1.4)-O-α-D-glucopyranosyl-(1.4)-O-α-D-glucopyranose/Maltotriose (8CI)/O-α-D-Glucopyranosyl-(1-4)-O-α-D-glucopyranosyl-(1-4)-D-glucose/Maltotriose hydrate/Maltotriose/Amylotriose/D-(+)-Maltotriose Hydrate/D-Glucose, O-α-D-glucopyranosyl-(1-4)-O-α-D-glucopyranosyl-(1-4)- (9CI)
958.9±65.0 °C at 760 mmHg
HS Code Reference
Personal Projective Equipment
For Reference Standard and R&D, Not for Human Use Directly.
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Tropomyosin is the most potent allergen of shrimp that can cause severe food allergy. However, to date, an effective approach to eliminate this allergenicity is still lacking. Glycation is a promising approach that can reduce the allergenicity of shrimp tropomyosin by destroying the epitopes; however, advanced glycation end products (AGEs) are also generated during glycation, which can function as neoallergens to strengthen the allergenicity; therefore, it is hard to tell how the glycation of an allergen with different saccharides affects the allergenicity via epitope loss and neoallergen generation. This study was aimed at the elucidation of how the glycation of tropomyosin (TM) with saccharides of different molecular sizes (glucose, maltose, and maltotriose) affected the allergenicity through epitope loss and the generation of neoallergns that belonged to advanced glycation end products (AGEs). Saccharides of higher molecular sizes (maltotriose) could lead to higher glycated TM than saccharides of smaller molecular sizes (glucose and maltose). Compared with TM, the TM glycated by glucose (TM-G) and maltotriose (TM-MTS) had lower allergenicity and contributed to weaker mouse allergy symptoms; on the other hand, the TM glycated by maltose (TM-M) had no significant impact on the allergenicity due to the generation of AGE-related neoallergens, which might offset the glycation-induced epitope loss. The glycation of TM by maltotriose led to lower generation of AGE neoallergens (e.g. CML) than that in the cases of glucose and maltose; therefore, maltotriose could be applied to desensitize TM-induced food allergy through glycation, and this could be a potential immunotherapy for shrimp allergy patients.
Glycation by saccharides of different molecular sizes affected the allergenicity of shrimp tropomyosin via epitope loss and the generation of advanced glycation end products.
Zhang Z1, Xiao H2, Zhou P3.
2019 Nov 1
Diastatic strains of Saccharomyces cerevisiae are common contaminants in beer fermentations and are capable of producing an extracellular STA1-encoded glucoamylase. Recent studies have revealed variable diastatic ability in strains tested positive for STA1, and here, we elucidate genetic determinants behind this variation. We show that poorly diastatic strains have a 1162-bp deletion in the promoter of STA1. With CRISPR/Cas9-aided reverse engineering, we show that this deletion greatly decreases the ability to grow in beer and consume dextrin, and the expression of STA1. New PCR primers were designed for differentiation of highly and poorly diastatic strains based on the presence of the deletion in the STA1 promoter. In addition, using publically available whole genome sequence data, we show that the STA1 gene is prevalent among the ‘Beer 2’/’Mosaic Beer’ brewing strains. These strains utilize maltotriose efficiently, but the mechanisms for this have been unknown. By deleting STA1 from a number of highly diastatic strains, we show here that extracellular hydrolysis of maltotriose through STA1 appears to be the dominant mechanism enabling maltotriose use during wort fermentation in STA1+ strains. The formation and retention of STA1 seems to be an alternative evolutionary strategy for efficient utilization of sugars present in brewer’s wort. The results of this study allow for the improved reliability of molecular detection methods for diastatic contaminants in beer and can be exploited for strain development where maltotriose use is desired.
Beer; Dextrin; Diastatic; Genome; Starch; Yeast
A deletion in the STA1 promoter determines maltotriose and starch utilization in STA1+ Saccharomyces cerevisiae strains.
Krogerus K1,2, Magalhães F3, Kuivanen J3,4, Gibson B3.
Saccharomyces eubayanus is the non-S. cerevisiae parent of the lager-brewing hybrid S. pastorianus. In contrast to most S. cerevisiae and Frohberg-type S. pastorianus strains, S. eubayanus cannot utilize the α-tri-glucoside maltotriose, a major carbohydrate in brewer’s wort. In Saccharomyces yeasts, utilization of maltotriose is encoded by the subtelomeric MAL gene family, and requires transporters for maltotriose uptake. While S. eubayanus strain CBS 12357T harbors four SeMALT genes which enable uptake of the α-di-glucoside maltose, it lacks maltotriose transporter genes. In S. cerevisiae, sequence identity indicates that maltotriose and maltose transporters likely evolved from a shared ancestral gene. To study the evolvability of maltotriose utilization in S. eubayanus CBS 12357T, maltotriose-assimilating mutants obtained after UV mutagenesis were subjected to laboratory evolution in carbon-limited chemostat cultures on maltotriose-enriched wort. An evolved strain showed improved maltose and maltotriose fermentation in 7 L fermenter experiments on industrial wort. Whole-genome sequencing revealed a novel mosaic SeMALT413 gene, resulting from repeated gene introgressions by non-reciprocal translocation of at least three SeMALT genes. The predicted tertiary structure of SeMalT413 was comparable to the original SeMalT transporters, but overexpression of SeMALT413 sufficed to enable growth on maltotriose, indicating gene neofunctionalization had occurred. The mosaic structure of SeMALT413 resembles the structure of S. pastorianus maltotriose-transporter gene SpMTY1, which has high sequences identity to alternatingly S. cerevisiae MALx1, S. paradoxus MALx1 and S. eubayanus SeMALT3. Evolution of the maltotriose transporter landscape in hybrid S. pastorianus lager-brewing strains is therefore likely to have involved mechanisms similar to those observed in the present study.
In vivo recombination of Saccharomyces eubayanus maltose-transporter genes yields a chimeric transporter that enables maltotriose fermentation.
Brouwers N1, Gorter de Vries AR1, van den Broek M1, Weening SM1, Elink Schuurman TD2, Kuijpers NGA2, Pronk JT1, Daran JG1.
2019 Apr 4;
Maltotriose is a ligosaccharide metabolite found in human urine.