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Fig. 1 | Bioresources and Bioprocessing

Fig. 1

From: Immobilization of transaminase from Bacillus licheniformis on copper phosphate nanoflowers and its potential application in the kinetic resolution of RS-α-methyl benzyl amine

Fig. 1

A Chromatogram of transaminase purification in anion exchange column; B SDS-PAGE analysis of different elution fractions of anion exchange chromatography*; C SEM images of sonication time optimization study on nanoflower synthesis, a 5 min, b 10 min, c 15 min, d 20 min, e 25 min, and f 30 min; D TA activity of hNFs synthesized at different sonication time intervals. *Proteins were separated on a 12% polyacrylamide gel in the presence of 1% SDS. Here, lane 1 represents marker proteins (molecular mass 203, 124, 80, 49.1, 34.8, 28.9, 20.6, 7.1 kDa), lane 2 depicts unbound fraction, lane 3 depicts 0.075 M NaCl elution fraction, lane 4 depicts 0.1 M NaCl elution fraction, lane 5 depicts 0.15 M NaCl elution fraction, lane 6 depicts 0.2 M NaCl elution fraction, lane 7 depicts 0.25 M NaCl elution fraction, lane 8 depicts 0.3 M NaCl elution fraction, lane 9 depicts 0.4 M NaCl elution fraction, lane 10 depicts 1.0 M NaCl elution fraction, and lane 11 depicts cell lysate

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