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Fig. 2 | Biotechnology for Biofuels and Bioproducts

Fig. 2

From: MpADC, an l-aspartate-α-decarboxylase, from Myzus persicae, that enables production of β-alanine with high yield by whole-cell enzymatic catalysis

Fig. 2

Analysis of MpADC expression and purified MpADC by SDS-PAGE and spectrometry. a SDS-PAGE analysis of protein expression in E. coli harboring pET-28a (+)-MpADC and different chaperone expression plasmids. Lane M: molecular weight protein standard; lanes 1, 3, 5, 7, 9, 11: the expression supernatant from the disrupted E.coli cell, which harboring pET-28a (+)-MpADC, pET-28a(+)-MpADC/pGrO7, pET-28a(+)-MpADC/pG-KJE8, pET-28a(+)-MpADC/pTf16, pET-28a(+)-MpADC/pKJE7, pET-28a(+)-MpADC/pGTf2, respectively; lanes 2, 4, 6, 8, 10, 12: the expression precipitation from the disrupted E. coil cell, harboring the plasmids with order above. The red box indicates the combination with highest soluble expression of MpADC. b SDS-PAGE analysis of purified MpADC. Lane M, molecular weight protein standard; lane 1: purified MpADC protein. c UV–visible spectra of the purified MpADC in 50 mM phosphate buffer (pH 7.0). The UV/visible spectrum from 300 to 500 nm was determined using an Agilent Bio Tek Synergy LX Multi-functional microplate detector. The presence of absorption peak with a λmax at 337 and 423 nm indicated by blue arrow

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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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