Title of article :
Preparation and characterization of maltosyl-sucrose isomers produced by transglycosylation of maltogenic amylase from Bacillus stearothermophilus
Author/Authors :
Lee، نويسنده , , Hye-Young and Kim، نويسنده , , Myo-Jeong and Baek، نويسنده , , Jin-Sook and Lee، نويسنده , , Hee-Seob and Cha، نويسنده , , Hyun-Ju and Lee، نويسنده , , Soo-Bok and Moon، نويسنده , , Tae-Wha and Seo، نويسنده , , Eun-Seong and Kim، نويسنده , , Doman and Park، نويسنده , , Cheon-Seok and Park، نويسنده , , Kwan-Hwa، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2003
Pages :
13
From page :
293
To page :
305
Abstract :
To develop a new transfer product of sucrose, sucrose was modified to maltosyl-sucrose using the transglycosylation activity of maltogenic amylase from Bacillus stearothermophilus (BSMA). The transglycosylation reaction was conducted with maltotriose and sucrose as the donor and acceptor, respectively. The presence of various sucrose transfer products was confirmed by thin layer chromatography (TLC) and high performance anion exchange chromatography (HPAEC). The sucrose transfer products were isolated by alkali-degradation followed by charcoal column chromatography using 20% (v/v) ethanol, then purified by ion exchange and Biogel P-2 gel permeation chromatographies. The structures of the major transfer products were determined to be 6G-α-maltosyl-sucrose (maltosyl-sucrose 1) and 6F-α-maltosyl-sucrose (maltosyl-sucrose 2) by LC-MS and 13C NMR. The mixture of maltosyl-sucrose 1 and 2 showed low sweetness, high hygroscopicity, low Maillard reactivity, and high acid and heat stability. Furthermore, it had an inhibitory effect on mutansucrase and water-insoluble glucan formation. These results indicated that the mixture of maltosyl-sucrose 1 and 2 is a suitable sugar substitute useful for various food products.
Keywords :
Bacillus stearothermophilus maltogenic amylase (BSMA) , transglycosylation , Maltosyl-sucrose , sucrose
Journal title :
Journal of Molecular Catalysis B Enzymatic
Serial Year :
2003
Journal title :
Journal of Molecular Catalysis B Enzymatic
Record number :
1709951
Link To Document :
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