Very Detailed Introduction to Maltase

Maltase is present in the small intestine and is a metabolite of natural starch. It is not a disaccharide substance originally synthesized by biological cells like sucrose. It has a good sweetness lower than that of sucrose and has good fermentation performance. Therefore, the industry for producing maltose using starch as a raw material has been developed very early. It can be broken down into D-glucose by α-glucosidase, so the animal can digest and absorb this sugar well. Some bacteria (such as Neisseria eningitidis) have an enzyme that decomposes maltose with phosphoric acid to produce β-D-glucose-1-phosphate. In addition, amylose-like polysaccharides were produced in maltose using glucose as a glucose-based donor.
Maltase was originally used as a name for an enzyme that hydrolyzes maltose to produce two molecules of glucose, but is now generally used as an alias for α-glucosidase acting on α-D-glucoside in combination with various glycosyl groups. It can cleave α-1,4 glycosidic bonds from the non-reducing end of the oligosaccharide substrate, release the glucose, or transfer the liberated glucose residue to the other substrate as the α-1,6 glycosidic bond. In this way, non-fermentable oligo-isomaltose (IMO), glycolipid or glycopeptide is obtained.
Alpha-glucosidase can be used as a saccharification enzyme preparation in the starch processing industry to produce high glucose syrup together with alpha-amylase. In addition, α-glucosidase, as a key enzyme preparation for industrial production of IMO, has received much attention from the food industry at home and abroad. Currently, the α-glucosidase used in industrial production is mainly derived from Aspergillus niger.
The optimization of a-glucosidase conditions and the preliminary study of enzymatic properties were carried out on a strain of Thermococcus siculi HJ21 isolated from the deep-sea hydrothermal vent. The intracellular fermentation time is 6h, and the extracellular fermentation time is 21h, which is more suitable for the production of α-glucosidase; its optimum enzyme temperature is 85°C, pH is 6.5, NaCl concentration is 2.5%; soluble starch, yeast powder and Peptone promotes enzyme production.The optimum temperature of the α-glucosidase is 100 ° C, the half-life of 90 ° C is 2 h; the pH of the optimum enzyme is 7.0, and the enzyme activity is relatively stable between pH 5.0 and 8.0; the thermal stability of the enzyme is not dependent. Ca2+, and Ca2+ inhibited the enzyme. Metal ions Cu2+, Al3+, and Ni2+ inhibited the enzyme. Hg2+ strongly inhibited the activity of the enzyme, while EDTA, Fe3+, and K+ activated the enzyme.
The α-glucosidase gene of T.siculiHJ21 was successfully cloned by PCR using T.siculiHJ21 chromosomal DNA as a template. The gene sequence showed that the open reading frame of the gene was 729 bp in size, and the encoded protein molecule contained 242 amino acid residues with a molecular weight of about 27.2 kDa. The homology alignment analysis with the published α-glucosidase gene sequence in the Genbank database showed that the α-glucosidase gene sequence of T.siculi HJ21 is closely related to the α-glucosidase of Thermococcus hydrothermalis. The homology reached 81% and the amino acid homology was 90%.
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