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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46524

Title: Functional Expression and Characterization of keratinase from Pseudomonas aeruginosa in Pichia pastoris.
Authors: Hsin-Hung Lin
Li-Jung Yin
Shann-Tzong Jiang
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: functional expression
Pseudomonas aeruginosa
keratinase
Pichia pastoris
Date: 2009
Issue Date: 2018-05-22T07:12:27Z
Publisher: Journal of Agricultural and Food Chemistry
Abstract: Abstract: Recombinant keratinase (rK) from Pseudomonas aeruginosa was secreted by Pichia pastoris SMD1168H with a final yield of 580 mg/L (1.03 kU/mL) after 72 h of induction. The rK was purified after nickel affinity chromatography and was stable at pH 6.0−9.0 and 10−60 °C. It was nonglycosylated protein with a molecular mass of 33 kDa and had an optimal pH and temperature at 8.0 and 60 °C, respectively. Ba2+, Ca2+, Mg2+, Mn2+, Zn2+, dithiothreitol, glutathione, and β-mercaptoethanol activated, while Cu2+, Fe2+, Hg2+, Fe3+, ethylene glycol tetraacetic acid, ethylene diamine tetraacetic acid, and p-chloromercuribenzoate inhibited its activity. rK could hydrolyze broad substrates and cleave hydrophobic and aromatic amino acids at P1 position, behaving as those from the wild type strain and E. coli transformant.
Relation: 57(12) pp.5321–5325
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46524
Appears in Collections:[食品科學系] 期刊論文

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