• Food Science and Biotechnology
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• 제16권1호
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• pp.127-132
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• 2007

[ ${\alpha},\;{\alpha}$ ]-Trehalose was efficiently modified by a transgalactosylation reaction of Escherichia coli ${\beta}-galactosidase$ using lactose as a donor to yield two galactosyl trehalose trisaccharides. The reaction products of trehalose by the enzyme were observed by thin layer chromatography (TLC) and high performance anion exchange chromatography (HPAEC) and were purified by BioGel P2 gel permeation chromatography and recycling preparative HPLC. Liquid chromatography-mass spectrometry (LC-MS) and ^{13}C$ nuclear magnetic resonance (NMR) analyses revealed that the structures of the main products were $6^2-{\beta}-D-galactosyl$ trehalose (1) and $4^2-{\beta}-D-galactosyl$ trehalose (2). A reaction of 30%(w/v) trehalose and 15%(w/v) lactose at pH 7.5 and $45^{\circ}C$ resulted in a total yield of approximately 27-30% based on the amount of trehalose used. The galactosyl trehalose products were not hydrolyzed by trehalose. In addition the mixture of transfer products (9:1 ratio of 1 to 2) showed higher thermal stability than glucose, lactose, and maltose, but less than trehalose, against heat treatment over $100^{\circ}C$ at pH 4 and 7. It also exhibited better thermal stability than sucrose at pH 4 alone.

• Food Science and Biotechnology
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• 제17권1호
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• pp.199-202
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• 2008

The effects of $\beta$-(1,6)-galactosyl trehalose trisaccharide ($\beta$-GT) that was preferentially produced by Escherichia coli $\beta$-galactosidase on cryo- and thermo-protections of protein were investigated with those of other sugars at the level of 8% (w/v). As compared to a control without sugar additive, $\beta$-GT effectively enhanced 32-54% of the cryoprotection of fish actomyosin against repeated freeze-thawing and frozen storage, and also 49% of the protection against thermal inactivation of pyrophosphatase, respectively. As a result, it was significantly more effective than sorbitol and trehalose in both cryoprotection and thermoprotection. Thus, $\beta$-GT would be possibly applied as a sugar substitute for cryo- and thermo-protective applications of food protein.