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Taka-amylase

Matsuura, Y., et al. Structure and possible catalytic residues of taka-amylase A. /. Bioehem. 95 ... [Pg.65]

Crystal-structure analysis of Taka amylase A gave similar results, in that it showed that it had an extended cleft which could accommodate six, or possibly seven, a-( 1 — 4)-linked glucose units and two oppositely placed acidic amino acids (Asp-206 and Glu-230) which could interact with the bound substrate similarly to Asp-52 and Glu-35 in lysozyme. [Pg.326]

An interesting observation is that an enzyme may exhibit different pH activity profiles for various neutral substrates. The explanation of this is that the enzyme binds or transforms such various substrates differently. For example. Taka amylase has different pH optima for long chain amyloses and for low molecular mass substrates. Some specific chemical modifications of the side chains of the enzyme may also alter the pH activity profiles. Kobayashi, Miura and Ichisima (1992) modified the lysine amino groups using bifimctional reagent o-phtalaldehyde, and observed a pronounced shift in the pH-dependence of ohgomaltoside hydrolysis. [Pg.320]

Kobayashi, M., Miura, M. and Ichishima, E. (1992) Modification of subsite Lys residue induced large increase in maltosidase activity of Taka-amylase A. Biochem. Biophys. Res. Comm., 183, 321-326. [Pg.336]

Fig. 5.—Structure of Hen-ovalbumin Glycopeptides GP-IV and GP-V (Ref. 96), GP-III-B (Ref. 97), and GP-VI (Ref. 98). [GP-V is identical to that of Taka-amylase A glycan (see Fig. 4) GP-IV and GP-V are identical to GP-5 and GP-6 glycopeptides from ovalbumin, as described by Conchie and Straehan.99]... Fig. 5.—Structure of Hen-ovalbumin Glycopeptides GP-IV and GP-V (Ref. 96), GP-III-B (Ref. 97), and GP-VI (Ref. 98). [GP-V is identical to that of Taka-amylase A glycan (see Fig. 4) GP-IV and GP-V are identical to GP-5 and GP-6 glycopeptides from ovalbumin, as described by Conchie and Straehan.99]...
Tada, S., Iimura, Y., Gomi, K., Takahashi, K., Hara, S., and Yoshizawa, K. (1989). Cloning and nucleotide sequence of the genomic Taka-amylase A gene of Aspergillus oryzae. Agric. Biol. Chem., 53, 593-399. [Pg.271]

PRODUCTS OF THE ENZYMIC DEGRADATION OF STARCH AND GLYCOGEN 295 4. Action of Taka-amylase ... [Pg.295]

The fractions MTII to MTVI were dissolved in water and treated with Taka-amylase (230 g. in 2500 ml. of water + toluene -f 2.5 g. of... [Pg.296]

Limit Dextrins from Different Starches with Taka-amylase... [Pg.297]

When acted upon by large amounts of amylases, the limit dextrins mentioned above are hydrolyzed further. Taka-amylase, for example, gave after prolonged action nearly 100% D-glucose. [Pg.301]

Taka-amylase contains phosphatase and will gradually set free the... [Pg.304]

See other pages where Taka-amylase is mentioned: [Pg.320]    [Pg.257]    [Pg.9]    [Pg.54]    [Pg.110]    [Pg.114]    [Pg.114]    [Pg.142]    [Pg.221]    [Pg.606]    [Pg.173]    [Pg.220]    [Pg.141]    [Pg.243]    [Pg.486]    [Pg.486]    [Pg.527]    [Pg.177]    [Pg.178]    [Pg.371]    [Pg.251]    [Pg.289]    [Pg.289]    [Pg.295]    [Pg.297]    [Pg.297]    [Pg.298]    [Pg.298]   
See also in sourсe #XX -- [ Pg.718 ]

See also in sourсe #XX -- [ Pg.29 ]

See also in sourсe #XX -- [ Pg.7 , Pg.34 , Pg.35 ]

See also in sourсe #XX -- [ Pg.491 ]

See also in sourсe #XX -- [ Pg.235 , Pg.280 , Pg.281 ]



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Action of Taka-amylase

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