Production of trehalose by intramolecular transglucosylation of maltose catalysed by a new enzyme from HB-8

Zdziebło, Anna; Synowiecki, J.

doi:10.1016/j.foodchem.2005.01.048

Cited by 20 publications

(14 citation statements)

References 14 publications

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“…A lower level of specific activity suggests that reduced enzyme productivity was caused not only by decreased amount of the cells in the growth medium but also by the diminished participation of maltose‐converting enzyme in cell proteins (Table 4). The effect of NaCl concentration in the growth medium of T. ruber on the cell yield and the enzyme productivity is similar to those determined for Thermus thermophilus (Zdzieblo and Synowiecki 2006).…”

Section: Resultssupporting

confidence: 79%

ACTIVITY AND PRIMARY CHARACTERIZATION OF ENZYME FROMTHERMUS RUBERCELLS CATALYZING CONVERSION OF MALTOSE INTO TREHALOSE

Sinkiewicz

Synowiecki

2009

Journal of Food Biochemistry

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Thermophilic bacteria Thermus ruber produces enzyme, which catalyzes the conversion of maltose into trehalose. The specific activity of the cell‐free extract from this bacteria growing without inducers was 0.028 U/mg protein and it was increased to up to 0.086 U/mg in the presence of 0.5% of maltose in the culture broth. The maximum degree of maltose conversion of about 90% was attained at 10% substrate concentration. The enzyme from Thermus ruber does not catalyze formation of trehalose from maltotetraose and maltopentaose. The optimum temperature for the enzyme activity was 65C. A maximum activity of the maltose conversion was performed at pH 6.5. The highest enzyme activity was achieved during cell cultivation at 55C on a media composed from 0.5% of peptone, 0.1% yeast extract and 0.5% of maltose or starch. PRACTICAL APPLICATIONS Trehalose is a chemically stable nonreducing disaccharide which can be used in food, cosmetics, medical and biotechnological industries. Extraction of this carbohydrate from yeast cells or other natural sources is unsuitable for trehalose production because of low process yield and high cost. Thus, the enzymatic methods of trehalose production are developed. In the current study the thermophilic bacteria Thermus ruber has been examined as a new source of the enzyme catalyzing conversion of maltose into trehalose.

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Section: Resultssupporting

confidence: 79%

ACTIVITY AND PRIMARY CHARACTERIZATION OF ENZYME FROMTHERMUS RUBERCELLS CATALYZING CONVERSION OF MALTOSE INTO TREHALOSE

Sinkiewicz

Synowiecki

2009

Journal of Food Biochemistry

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“…In addition, the yields of the exogenous enzymes expressed in Escherichia coli have also been studied and optimized . However, the current studies on TreS have only been limited to gene cloning and enzymatic property characterization (Li et al, 2012;Ryu et al, 2010;Zdziebło and Synowiecki, 2006;Wei et al, 2013;Kushwaha et al, 2011;Yoshiyama et al, 2014) and little is known about the transcription and translation process of the TreS genes. Moreover, there are no reports on the comparison of the expression of TreS genes from different sources and expression vectors with distinct promoters.…”

Section: Introductionmentioning

confidence: 99%

Cloning, expression and activity optimization of trehalose synthase from Thermus thermophilus HB27

Sun

Feng

et al. 2015

Chemical Engineering Science

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“…This multifunctional food ingredient does not caramelize and does not undergo Maillard reactions, is safe for human consumption and has been accepted by the European regulation system (Richards et al 2002;Schiraldi et al 2002). Trehalose may be used in many products including beverages, chocolate and sugar confectionery, bakery, dairy and fruit products and as a cryoproteotectant in frozen foods (Zdzieblo and Synowiecki 2006).…”

Section: Introductionmentioning

confidence: 99%

Characterization of trehalose synthase from Corynebacterium nitrilophilus NRC

Asker

Ramadan

El-Aal

et al. 2009

World J Microbiol Biotechnol

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Trehalose synthase (TSII) from Corynebacterium nitrilophilus NRC was successively purified by ammonium sulphate precipitation, ion exchange chromatography on DEAE-cellulose and gel filtration chromatography on Sephadex G-100 columns. The specific activity of the trehalose synthase was increased *200-fold, from 0.14 U mg -1 protein to 28.3 U mg -1 protein. TSII was found to be a monomeric protein with a molecular weight of 67-69 kDa. Characterization of the enzyme exhibited optimum pH and temperature were 7.5 and 35°C, respectively. The purified enzyme was stable from pH 6.6 to 7.8 and able to prolong its thermal stability up to 35°C. The enzyme activity was inhibited strongly by Zn 2? , Hg 2? and Cu 2? and moderately by Ba 2? , Fe 2? , Pb 2? and Ni 2? . Other metal ions Ca 2? , Mg 2? , Co 2? , Mn 2? and EDTA had almost no effect.

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Production of trehalose by intramolecular transglucosylation of maltose catalysed by a new enzyme from HB-8

Cited by 20 publications

References 14 publications

ACTIVITY AND PRIMARY CHARACTERIZATION OF ENZYME FROMTHERMUS RUBERCELLS CATALYZING CONVERSION OF MALTOSE INTO TREHALOSE

ACTIVITY AND PRIMARY CHARACTERIZATION OF ENZYME FROMTHERMUS RUBERCELLS CATALYZING CONVERSION OF MALTOSE INTO TREHALOSE

Cloning, expression and activity optimization of trehalose synthase from Thermus thermophilus HB27

Characterization of trehalose synthase from Corynebacterium nitrilophilus NRC

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