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. 2001 Apr;125(4):1723–1731. doi: 10.1104/pp.125.4.1723

Table I.

Isoamylase purification

Extract Origin Yield
Purification Factor
Total Activitya
sta8 + sta8 + sta8 +
%
Crude extract 100 100 0 0 225 322
Protamine sulfate 74 65 1, 7 1, 3 167 210
Ammonium sulfate 46 40 2, 4 1, 6 105 130
Gel permeation (52–65) 17 9, 9 55
Gel permeation (58–66) 19 9, 9 42
Anion exchange (19–20) 2, 5 140 8, 2
Anion exchange (15–16) 4, 5 77 10, 2
a

 Purification was from 4 × 1010 cells. Debranching activity corresponds to micromoles of maltotriose equivalents produced per hour from amylopectin for the whole fraction in study. After the gel permeation step, wild-type isoamylase was free of interfering starch hydrolytic activity, whereas trace amounts of α-amylase can be detected by zymograms in the sta8 semipurified fractions.