Screening of novel high-stability alkaline protease mutants
The invention belongs to the technical field of enzyme genetic engineering, and relates to screening of novel high-stability alkaline protease mutants. The high-stability mutants of alkaline proteasederived from bacillus clausii are screened by error-prone PCR. According to sequencing, The genes of...
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| creator | QIU YUEYUE LI XUE WANG HONGBIN WANG YUYING LIU YIHAN LU FUPING |
| description | The invention belongs to the technical field of enzyme genetic engineering, and relates to screening of novel high-stability alkaline protease mutants. The high-stability mutants of alkaline proteasederived from bacillus clausii are screened by error-prone PCR. According to sequencing, The genes of the mutants respectively have GAT at site 747-749, GTT at site 859-861 and CTG at site 955-957; thecorresponding sequence mutation is that the site 165 mutates to Asp, the site 203 mutates to Val and the site 235 mutates to Leu respectively; and after fermentation for 48 hours, the enzyme activityvalues of the mutant fermentation broths are respectively 30U/mL, 41U/mL and 35U/mL, which are respectively 11%, 51% and 30% higher than enzyme activity of a fermentation broth with expression of a wild-type alkaline protease aprE recombinant strain. After the obtained fermentation broth is subjected to ultrafiltration and incubation at 40 DEG C for 48 hours, the enzyme activity retention rate ofthe alkaline protease mutan |
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The high-stability mutants of alkaline proteasederived from bacillus clausii are screened by error-prone PCR. According to sequencing, The genes of the mutants respectively have GAT at site 747-749, GTT at site 859-861 and CTG at site 955-957; thecorresponding sequence mutation is that the site 165 mutates to Asp, the site 203 mutates to Val and the site 235 mutates to Leu respectively; and after fermentation for 48 hours, the enzyme activityvalues of the mutant fermentation broths are respectively 30U/mL, 41U/mL and 35U/mL, which are respectively 11%, 51% and 30% higher than enzyme activity of a fermentation broth with expression of a wild-type alkaline protease aprE recombinant strain. 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The high-stability mutants of alkaline proteasederived from bacillus clausii are screened by error-prone PCR. According to sequencing, The genes of the mutants respectively have GAT at site 747-749, GTT at site 859-861 and CTG at site 955-957; thecorresponding sequence mutation is that the site 165 mutates to Asp, the site 203 mutates to Val and the site 235 mutates to Leu respectively; and after fermentation for 48 hours, the enzyme activityvalues of the mutant fermentation broths are respectively 30U/mL, 41U/mL and 35U/mL, which are respectively 11%, 51% and 30% higher than enzyme activity of a fermentation broth with expression of a wild-type alkaline protease aprE recombinant strain. 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The high-stability mutants of alkaline proteasederived from bacillus clausii are screened by error-prone PCR. According to sequencing, The genes of the mutants respectively have GAT at site 747-749, GTT at site 859-861 and CTG at site 955-957; thecorresponding sequence mutation is that the site 165 mutates to Asp, the site 203 mutates to Val and the site 235 mutates to Leu respectively; and after fermentation for 48 hours, the enzyme activityvalues of the mutant fermentation broths are respectively 30U/mL, 41U/mL and 35U/mL, which are respectively 11%, 51% and 30% higher than enzyme activity of a fermentation broth with expression of a wild-type alkaline protease aprE recombinant strain. After the obtained fermentation broth is subjected to ultrafiltration and incubation at 40 DEG C for 48 hours, the enzyme activity retention rate ofthe alkaline protease mutan</abstract><oa>free_for_read</oa></addata></record> |
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| subjects | BEER BIOCHEMISTRY CHEMISTRY COMPOSITIONS THEREOF CULTURE MEDIA ENZYMOLOGY METALLURGY MICROBIOLOGY MICROORGANISMS OR ENZYMES MUTATION OR GENETIC ENGINEERING PROCESSES USING MICROORGANISMS PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS SPIRITS VINEGAR WINE |
| title | Screening of novel high-stability alkaline protease mutants |
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