Identification of a New Serine Alkaline Peptidase from the Moderately Halophilic <i>Virgibacillus natechei</i> sp. nov., Strain FarD<sup>T</sup> and its Application as Bioadditive for Peptide Synthesis and Laundry Detergent Formulations

<div>(a) Time course of <i>Virgibacillus natechei</i> strain FarD<sup>T</sup> cell growth (Δ) and peptidase production (▲). Cell growth was monitored by measuring the absorbance at 600 nm and was converted to cell dry weight (g/L). Each point represents the mean of three independent experiments. (b) 12% SDS-PAGE of the purified peptidase SAPV. Lane 1, purified SAPV (50 <i>µ</i>g) obtained after ZORBAX PSM 300 HPLC chromatography (Rt = 8.676 min). Lane 2, Amersham LMW protein marker. (c, d) Zymogram caseinolytic activity staining of peptidase activity. Lane 1, the purified peptidase SAPV (50 <i>µ</i>g).</div>

BioMed Research International

fig1

Figure 1

Figure 1: Identification of a New Serine Alkaline Peptidase from the Moderately Halophilic <i>Virgibacillus natechei</i> sp. nov., Strain FarD<sup>T</sup> and its Application as Bioadditive for Peptide Synthesis and Laundry Detergent Formulations 

Figure 1 | Identification of a New Serine Alkaline Peptidase from the Moderately Halophilic Virgibacillus natechei sp. nov., Strain FarDT and its Application as Bioadditive for Peptide Synthesis and Laundry Detergent Formulations 