Wheat, beta amylase

Sulfhydryl groups have also been reported to be essential for the action of crystalline, wheat beta-amylase, and titration of the purified enzyme with iodoacetic acid suggested that there were 3.6—3.8 SH groups per molecule. 

The amino acid compositions of the beta-amylase from sweet potato, soya bean, wheat, and malted sorghum have been determined, and are shown in Table XIII. These results may suggest that the beta-amylase from these different sources differs in structure. This is, perhaps, not surprising, but it should be noted that the sorghum amylase contained 9% of pentose, and the important, sulfiir-containing amino acid cysteine was not reported and the soya-bean enzyme still contained traces of aipba-amylase and phosphatase. The sequence of amino acids, or the three-dimensional structure of any... 

Table XIV shows the results of the few reports of the molecular size of beta-amylase. No crystallized enzyme from cereals or beans has yet been examined by physical techniques. There is also a problem regarding the important, sweet-potato enzyme the only full report in the literature has been contradicted, and it has been suggested, without experimental details, that subunits of beta-amylase exist. In addition, in the case of cereal fcefo-amylases, where there is the complication of free and bound enzyme, the wheat and malted-barley enzyme has been reported to contain...

C = crystallized P = purified. Parentheses indicate an assumed value. Calculated from S h Dto, and V. Range of components reported to have beta-amylase activity molecular weights, only, estimated from Sso- Three distinct components firom barley malt. From sedimentation equilibrium measurements. Value quoted from a personal communication from M. Burr and D. Yphantis. Three distinct components firom wheat. 

Wheat beta-limit dextrin Sepherogel-TSK 3000SW HjO a-Amylase h study... 

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