glutaminase/pòm tè

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Effects of glutenin and gliadin modified by protein-glutaminase on pasting, rheological properties and microstructure of potato starch.

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Glutenin and gliadin were treated with protein-glutaminase in order to obtain soluble glutenin (PG-Glu) and gliadin (PG-Gli). PG-Glu or PG-Gli was added to potato starch at various concentrations (0.5%, 1.0%, and 1.5% of starch weight, w/w), and the physicochemical properties and microstructure of

Effect of glutenin and gliadin modified by protein-glutaminase on retrogradation properties and digestibility of potato starch.

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The glutenin (Glu) and gliadin (Gli) were modified by protein-glutaminase (PG) to obtain soluble glutenin (PG-Glu) and gliadin (PG-Gli), and PG-Glu or PG-Gli was added to potato starch (PS) according to different amounts (0.5%, 1.0%, and 1.5%, based on dry starch weight, w/w) to explore the effect

Molecular cloning, structural modeling and characterization of a novel glutaminase-free L-asparaginase from Cobetia amphilecti AMI6.

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The exploration of new sources of L-asparaginase with low glutaminase activity is of great interest in both medical and food applications. In the current study, a novel L-asparaginase gene (CobAsnase) from halotolerant Cobetia amphilecti AMI6 was cloned and over-expressed in Escherichia coli. The

Gene cloning and expression of the l-asparaginase from Bacillus cereus BDRD-ST26 in Bacillus subtilis WB600.

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l-Asparaginase (ASN; EC 3.5.1.1) shows great commercial value because of its ability to reduce toxic levels of acrylamide in foods. To achieve high-efficiency production of l-asparaginase, an open reading frame of 978 bp encoding asparaginase (BcA) was amplified from Bacillus cereus BDRD-ST26,

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