Partial purification and characterization of nitrophenyl maltosaccharide-hydrolyzing enzymes from Lactobacillus sp. no. 26X

✍ Scribed by Hans Bender

• Publisher: Elsevier Science
• Year: 1995
• Tongue: English
• Weight: 423 KB
• Volume: 277
• Category: Article
• ISSN: 0008-6215
• DOI: 10.1016/0008-6215(95)00216-g

✦ Synopsis

Two nitrophenyl maltosaccharide-hydrolyzing enzymes were partially purified from l_zwtobacillus sp. no. 26X. One of the enzymes, designated nitrophenyl a-maltosidase, being a homotetramer with M r ca. 163,000, preferentially acted on p-nitrophenyl a-maltoside. The hydrolysis rates decreased with increasing length of the nitrophenyl maltosaccharides. Maltose, maltotriose, maltotetraose, and p-nitrophenyl a-D-glucopyranoside were scarcely attacked. The enzyme mainly hydrolyzed the bond between the nitrophenyl group and the sugar moiety, and oand p-nitrophenylated substrates were hydrolyzed equally well. The second enzyme, designated nitrophenyl a-o-glucosidase, was presumably a homodimer with M r ca. 51,000, and was specific for p-nitrophenyl a-o-glucopyranoside. The usefulness of the nitrophenyl a-maltosidase for coupled enzymic assays for the decycling maltodextrinase and alpha-amylases with nitrophenyl maltosaccharides as the substrates is discussed.