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Fig. 6 | Microbial Cell Factories

Fig. 6

From: Heterologous expression of an α-amylase inhibitor from common bean (Phaseolus vulgaris) in Kluyveromyces lactis and Saccharomyces cerevisiae

Fig. 6

Purification of recombinant αAI from culture supernatants of K. lactis YCT390/αAI-OPT. SDS-PAGE and western blot of a fractions purified by anion exchange chromatography from K. lactis YCT390/αAI-OPT strain 68A: protein unbound to DEAE-Sepharose (lane 1), protein bound to DEAE-Sepharose (lane 2); and b fractions purified by affinity chromatography: unbound proteins to α-amylase-Sepharose (lane 3), and proteins bound to α-amylase-Sepharose (lane 4). Pure Pinto-αAI (200 ng) was used as a positive control (+C). Molecular markers are shown in kilodaltons at left. c Inhibition of porcine pancreatic α-amylase by purified fractions containing unbound proteins to DEAE-Sepharose (lane 1), bound proteins to DEAE-Sepharose (lane 2), unbound proteins to α-amylase-Sepharose (lane 3), and bound proteins to α-amylase-Sepharose (lane 4). Untransformed strain YCT390 was used as a negative control (−C) and pure Pinto-αAI (200 ng) was used as a positive control (+C). Data from triplicate experiments were expressed as the average ± standard error

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Microbial Cell Factories

ISSN: 1475-2859

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