Strategy for efficient production of recombinant Staphylococcus epidermidis lipase in Bacillus subtilis

Chen, Po-Ting; Chen, Yi-Chung; Lin, Yong-Yang; Su, Heng-Hui

doi:10.1016/j.bej.2015.07.008

Cited by 10 publications

(2 citation statements)

References 41 publications

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“…The enzyme production through fermentation was similar to that through shake flask cultivation. Compared with that in previous studies (Chen et al 2007(Chen et al , 2015Su et al 2017b), the yield of keratinase was the highest when using LB broth as the fermentation medium.…”

Section: Batch Fermentation Of Kerp-producing B Subtiliscontrasting

confidence: 65%

“…For secretion, proteins need to be guided by the signal peptide. The appropriate signal peptide could enhance the secretion efficiency even though the original signal peptide may not be the best signal peptide (Chen et al 2015). Therefore, screening of the signal peptide must be considered during the construction of the expression vector for the host.…”

Section: Enhancement Of the Kerp Secretion In B Subtilismentioning

confidence: 99%

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Characterization and overexpression of a novel keratinase from Bacillus polyfermenticus B4 in recombinant Bacillus subtilis

Dong

Chang

Chen

2017

Bioresour. Bioprocess.

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Background: Keratins, insoluble proteins with a robust structure, are a major component of epidermal tissue and appendages such as hair, feathers, nails, and walls. Keratinous waste mainly emanates from poultry and leather industries, thereby severely contaminating the environment. Keratinase can lyse proteins with robust cross-linked structures, such as keratin, and can hence be used in animal feed, fertilizer, detergent, leather, pharmaceutical, and cosmetic industries. Bacillus polyfermenticus B4, isolated from feather compost, secretes keratinase to metabolize feathers. Hence, this study aimed to investigate the enzymatic characteristics and recombinant production of keratinase from B. polyfermenticus B4.Methods: A novel keratinase KerP was isolated from B. polyfermenticus B4 and overexpressed in B. subtilis PT5, via the T7 promoter. Results:The highest keratinolytic activity of recombinant KerP was observed at pH 9.0 and 60 °C. Enzyme activity was enhanced with Fe

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Section: Batch Fermentation Of Kerp-producing B Subtiliscontrasting

confidence: 65%

Section: Enhancement Of the Kerp Secretion In B Subtilismentioning

confidence: 99%