Hydrolysis of low-molecular-weight oligosaccharides and oligosaccharide alditols by pig intestinal sucrase/isomaltase and glucosidase/maltase

Carbohydrate Research

Volumn 326, Issue 4, 2000, Pages 264-276

  Hertel, Sabine ^a   Heinz, Fritz ^b   Vogel, Manfred ^a  

^a Entwickl Serv Sudzucker AG M   (Germany)

^b Zentrum Biochemie   (Germany)

Author keywords

Affinity to monomeric units of substrates; Characteristic of active sites; Enzyme specificity; Glucosidase; Isomaltase; Maltase; Pig intestinal sucrase

Indexed keywords

ALPHA GLUCOSIDASE; OLIGO 1,6 GLUCOSIDASE; OLIGOSACCHARIDE; SUCRASE;

ANIMAL TISSUE; ARTICLE; BIODEGRADATION; CARBOHYDRATE SYNTHESIS; CHEMICAL STRUCTURE; CONFORMATION; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; HYDROLYSIS; INTESTINE EPITHELIUM; NONHUMAN; PRIORITY JOURNAL; SWINE;

ALPHA-GLUCOSIDASES; ANIMALS; BINDING SITES; CARBOHYDRATE CONFORMATION; CARBOHYDRATE SEQUENCE; HUMANS; HYDROLYSIS; INTESTINAL MUCOSA; KINETICS; MICROVILLI; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; OLIGOSACCHARIDES; SUBSTRATE SPECIFICITY; SUCRASE-ISOMALTASE COMPLEX; SUGAR ALCOHOLS;

SUS SCROFA;

EID: 0034734004     PISSN: 00086215     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6215(00)00008-2     Document Type: Article

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