Summary
A sequence for the fractionation of the amylasic components from a malted barley extract is proposed using two salt-promoted, adsorption processes: thiophilic interaction chromatography (TIC) and hydrophobic interaction chromatography (HIC).
Two fractions containing α-amylase activity were recovered during the thiophilic chromatography; the first was resolved in to α-amylase I and β-amylase I by HIC on a phenyl-sepharose column; an enrichment factor of 32 was achieved for α-amylase I. The other amylasic component eluted from the thiophilic gel was characterized as α-amylase II. Although the adsorption of malt amylases on phenylsepharose and the thiophilic adsorbent is salt promoted, the interactions involved in each case are clearly distinguished by the different behaviour and disparate salt effects.
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Pazos, C., Franco-Fraguas, L. & Batista-Viera, F. Salt promoted adsorption chromatography of malted barley amylases. Chromatographia 38, 232–234 (1994). https://doi.org/10.1007/BF02290342
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DOI: https://doi.org/10.1007/BF02290342