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首页> 外文期刊>Carbohydrate research >Hydrolysis of low-molecular-weight oligosaccharides and oligosaccharide alditols by pig intestinal sucrase/isomaltase and glucosidase/maltase
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Hydrolysis of low-molecular-weight oligosaccharides and oligosaccharide alditols by pig intestinal sucrase/isomaltase and glucosidase/maltase

机译：猪肠蔗糖酶/异麦芽糖酶和葡糖苷酶/麦芽糖酶水解低分子量寡糖和寡糖醛糖醇

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摘要

The ability of purified pig intestinal sucrase/isomaltase (SI;EC 3.2.1.10/48)and glucosidase/maltase (GM;EC 3.2.1.20)to hydrolyze di- and oligosaccharides consisting of D-glucose and D-fructose residues and the corresponding alditols was studied. The products,after incubation,reflect different binding patterns at both catalytic sites of SI. The active site of the sucrese subunit cleaves #alpha#,#beta#-(1 -> 2) glycosidic bonds,and only two monomer units of the substrates bind with favorable affinity. Oligosaccharides and reduced oligosaccharides containing #alpha#-(1 -> 6) and #alpha#-(1 -> 1) glycosidic bonds are hydrolyzed by isomaltase,and for the active site of this subunit more than two subsites were postulated. Moreover,different binding sites for various aglycons seem to exist for isomaltase. Oligosaccharide alcohols are cleaved at lower rates if the reduced sugar residue occupies the aglycon binding site. GM also hydrolyzes #alpha#-(1 -> 1) linkages,but at a lower rate. The enzyme has the ability to bind compounds containing residues other than D-glucose. There are indications for similarities between GM and the isomaltase subunit of SI in the binding mode of oligosaccharides.
机译：纯化的猪肠蔗糖酶/异麦芽糖酶（SI; EC 3.2.1.10/48）和葡糖苷酶/麦芽糖酶（GM; EC 3.2.1.20）水解由D-葡萄糖和D-果糖残基组成的二糖和寡糖的能力研究了糖醇。温育后的产物在SI的两个催化位点处反映不同的结合模式。蔗糖亚基的活性位点切割#alpha＃，＃beta＃-（1-> 2）糖苷键，并且底物中只有两个单体单元以良好的亲和力结合。含有#alpha＃-（1-> 6）和#alpha＃-（1-> 1）糖苷键的寡糖和还原型寡糖被异麦芽酮糖水解酶水解，并为该亚基的活性位点假定了两个以上的亚位点。而且，对于异麦芽糖酶，各种糖苷配基的不同结合位点似乎存在。如果还原的糖残基占据糖苷配基结合位点，则寡糖醇以较低的速率裂解。 GM还水解#alpha＃-（1-> 1）键，但速率较低。该酶具有结合含有D-葡萄糖以外的残基的化合物的能力。有迹象表明，在寡糖的结合模式下，GM和SI的异麦芽糖酶亚基之间存在相似性。

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