ANCUT1, a novel thermoalkaline cutinase from Aspergillus nidulans and its application on hydroxycinnamic acids lipophilization
Biotechnol Lett. 2024 Feb 28. doi: 10.1007/s10529-024-03467-2. Online ahead of print.ABSTRACTOne of the four cutinases encoded in the Aspergillus nidulans genome, ANCUT1, is described here. Culture conditions were evaluated, and it was found that this enzyme is produced only when cutin is present in the culture medium, unlike the previously described ANCUT2, with which it shares 62% amino acid identity. The differences between them include the fact that ANCUT1 is a smaller enzyme, with experimental molecular weight and pI values of 22 kDa and 6, respectively. It shows maximum activity at pH 9 and 60 °C under assayed condi...
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Carolina Pe ña-Montes Eva Berm údez-García Denise Castro-Ochoa Fernanda Vega-P érez Katia Esqueda-Dom ínguez Jos é Augusto Castro-Rodríguez Augusto Gonz ález-Canto Laura Segoviano-Reyes Arturo Navarro-Oca ña Amelia Farr és Source Type: research

Recycling selectable markers via Cre/loxP system for constructing Komagataella phaffii strains co-expressing multiple proteins
CONCLUSIONS: With easy manipulation, the method was effective in recycling of the selectable markers, and consequently two protein genes were sequential integrated chromosomally and successfully co-expressed in the yeast.PMID:38416308 | DOI:10.1007/s10529-024-03466-3 (Source: Biotechnology Letters)
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Weixian Wang Minghai Han Guofei Zhu Xiaohui Liu Tianming Zhao Xiaoyan Ma Xun Gong Cunbin Xu Source Type: research

ANCUT1, a novel thermoalkaline cutinase from Aspergillus nidulans and its application on hydroxycinnamic acids lipophilization
Biotechnol Lett. 2024 Feb 28. doi: 10.1007/s10529-024-03467-2. Online ahead of print.ABSTRACTOne of the four cutinases encoded in the Aspergillus nidulans genome, ANCUT1, is described here. Culture conditions were evaluated, and it was found that this enzyme is produced only when cutin is present in the culture medium, unlike the previously described ANCUT2, with which it shares 62% amino acid identity. The differences between them include the fact that ANCUT1 is a smaller enzyme, with experimental molecular weight and pI values of 22 kDa and 6, respectively. It shows maximum activity at pH 9 and 60 °C under assayed condi...
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Carolina Pe ña-Montes Eva Berm údez-García Denise Castro-Ochoa Fernanda Vega-P érez Katia Esqueda-Dom ínguez Jos é Augusto Castro-Rodríguez Augusto Gonz ález-Canto Laura Segoviano-Reyes Arturo Navarro-Oca ña Amelia Farr és Source Type: research

Recycling selectable markers via Cre/loxP system for constructing Komagataella phaffii strains co-expressing multiple proteins
CONCLUSIONS: With easy manipulation, the method was effective in recycling of the selectable markers, and consequently two protein genes were sequential integrated chromosomally and successfully co-expressed in the yeast.PMID:38416308 | DOI:10.1007/s10529-024-03466-3 (Source: Biotechnology Letters)
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Weixian Wang Minghai Han Guofei Zhu Xiaohui Liu Tianming Zhao Xiaoyan Ma Xun Gong Cunbin Xu Source Type: research

ANCUT1, a novel thermoalkaline cutinase from Aspergillus nidulans and its application on hydroxycinnamic acids lipophilization
Biotechnol Lett. 2024 Feb 28. doi: 10.1007/s10529-024-03467-2. Online ahead of print.ABSTRACTOne of the four cutinases encoded in the Aspergillus nidulans genome, ANCUT1, is described here. Culture conditions were evaluated, and it was found that this enzyme is produced only when cutin is present in the culture medium, unlike the previously described ANCUT2, with which it shares 62% amino acid identity. The differences between them include the fact that ANCUT1 is a smaller enzyme, with experimental molecular weight and pI values of 22 kDa and 6, respectively. It shows maximum activity at pH 9 and 60 °C under assayed condi...
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Carolina Pe ña-Montes Eva Berm údez-García Denise Castro-Ochoa Fernanda Vega-P érez Katia Esqueda-Dom ínguez Jos é Augusto Castro-Rodríguez Augusto Gonz ález-Canto Laura Segoviano-Reyes Arturo Navarro-Oca ña Amelia Farr és Source Type: research

Recycling selectable markers via Cre/loxP system for constructing Komagataella phaffii strains co-expressing multiple proteins
CONCLUSIONS: With easy manipulation, the method was effective in recycling of the selectable markers, and consequently two protein genes were sequential integrated chromosomally and successfully co-expressed in the yeast.PMID:38416308 | DOI:10.1007/s10529-024-03466-3 (Source: Biotechnology Letters)
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Weixian Wang Minghai Han Guofei Zhu Xiaohui Liu Tianming Zhao Xiaoyan Ma Xun Gong Cunbin Xu Source Type: research

ANCUT1, a novel thermoalkaline cutinase from Aspergillus nidulans and its application on hydroxycinnamic acids lipophilization
Biotechnol Lett. 2024 Feb 28. doi: 10.1007/s10529-024-03467-2. Online ahead of print.ABSTRACTOne of the four cutinases encoded in the Aspergillus nidulans genome, ANCUT1, is described here. Culture conditions were evaluated, and it was found that this enzyme is produced only when cutin is present in the culture medium, unlike the previously described ANCUT2, with which it shares 62% amino acid identity. The differences between them include the fact that ANCUT1 is a smaller enzyme, with experimental molecular weight and pI values of 22 kDa and 6, respectively. It shows maximum activity at pH 9 and 60 °C under assayed condi...
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Carolina Pe ña-Montes Eva Berm údez-García Denise Castro-Ochoa Fernanda Vega-P érez Katia Esqueda-Dom ínguez Jos é Augusto Castro-Rodríguez Augusto Gonz ález-Canto Laura Segoviano-Reyes Arturo Navarro-Oca ña Amelia Farr és Source Type: research

Recycling selectable markers via Cre/loxP system for constructing Komagataella phaffii strains co-expressing multiple proteins
CONCLUSIONS: With easy manipulation, the method was effective in recycling of the selectable markers, and consequently two protein genes were sequential integrated chromosomally and successfully co-expressed in the yeast.PMID:38416308 | DOI:10.1007/s10529-024-03466-3 (Source: Biotechnology Letters)
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Weixian Wang Minghai Han Guofei Zhu Xiaohui Liu Tianming Zhao Xiaoyan Ma Xun Gong Cunbin Xu Source Type: research

ANCUT1, a novel thermoalkaline cutinase from Aspergillus nidulans and its application on hydroxycinnamic acids lipophilization
Biotechnol Lett. 2024 Feb 28. doi: 10.1007/s10529-024-03467-2. Online ahead of print.ABSTRACTOne of the four cutinases encoded in the Aspergillus nidulans genome, ANCUT1, is described here. Culture conditions were evaluated, and it was found that this enzyme is produced only when cutin is present in the culture medium, unlike the previously described ANCUT2, with which it shares 62% amino acid identity. The differences between them include the fact that ANCUT1 is a smaller enzyme, with experimental molecular weight and pI values of 22 kDa and 6, respectively. It shows maximum activity at pH 9 and 60 °C under assayed condi...
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Carolina Pe ña-Montes Eva Berm údez-García Denise Castro-Ochoa Fernanda Vega-P érez Katia Esqueda-Dom ínguez Jos é Augusto Castro-Rodríguez Augusto Gonz ález-Canto Laura Segoviano-Reyes Arturo Navarro-Oca ña Amelia Farr és Source Type: research

Recycling selectable markers via Cre/loxP system for constructing Komagataella phaffii strains co-expressing multiple proteins
CONCLUSIONS: With easy manipulation, the method was effective in recycling of the selectable markers, and consequently two protein genes were sequential integrated chromosomally and successfully co-expressed in the yeast.PMID:38416308 | DOI:10.1007/s10529-024-03466-3 (Source: Biotechnology Letters)
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Weixian Wang Minghai Han Guofei Zhu Xiaohui Liu Tianming Zhao Xiaoyan Ma Xun Gong Cunbin Xu Source Type: research

ANCUT1, a novel thermoalkaline cutinase from Aspergillus nidulans and its application on hydroxycinnamic acids lipophilization
Biotechnol Lett. 2024 Feb 28. doi: 10.1007/s10529-024-03467-2. Online ahead of print.ABSTRACTOne of the four cutinases encoded in the Aspergillus nidulans genome, ANCUT1, is described here. Culture conditions were evaluated, and it was found that this enzyme is produced only when cutin is present in the culture medium, unlike the previously described ANCUT2, with which it shares 62% amino acid identity. The differences between them include the fact that ANCUT1 is a smaller enzyme, with experimental molecular weight and pI values of 22 kDa and 6, respectively. It shows maximum activity at pH 9 and 60 °C under assayed condi...
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Carolina Pe ña-Montes Eva Berm údez-García Denise Castro-Ochoa Fernanda Vega-P érez Katia Esqueda-Dom ínguez Jos é Augusto Castro-Rodríguez Augusto Gonz ález-Canto Laura Segoviano-Reyes Arturo Navarro-Oca ña Amelia Farr és Source Type: research

Recycling selectable markers via Cre/loxP system for constructing Komagataella phaffii strains co-expressing multiple proteins
CONCLUSIONS: With easy manipulation, the method was effective in recycling of the selectable markers, and consequently two protein genes were sequential integrated chromosomally and successfully co-expressed in the yeast.PMID:38416308 | DOI:10.1007/s10529-024-03466-3 (Source: Biotechnology Letters)
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Weixian Wang Minghai Han Guofei Zhu Xiaohui Liu Tianming Zhao Xiaoyan Ma Xun Gong Cunbin Xu Source Type: research

ANCUT1, a novel thermoalkaline cutinase from Aspergillus nidulans and its application on hydroxycinnamic acids lipophilization
Biotechnol Lett. 2024 Feb 28. doi: 10.1007/s10529-024-03467-2. Online ahead of print.ABSTRACTOne of the four cutinases encoded in the Aspergillus nidulans genome, ANCUT1, is described here. Culture conditions were evaluated, and it was found that this enzyme is produced only when cutin is present in the culture medium, unlike the previously described ANCUT2, with which it shares 62% amino acid identity. The differences between them include the fact that ANCUT1 is a smaller enzyme, with experimental molecular weight and pI values of 22 kDa and 6, respectively. It shows maximum activity at pH 9 and 60 °C under assayed condi...
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Carolina Pe ña-Montes Eva Berm údez-García Denise Castro-Ochoa Fernanda Vega-P érez Katia Esqueda-Dom ínguez Jos é Augusto Castro-Rodríguez Augusto Gonz ález-Canto Laura Segoviano-Reyes Arturo Navarro-Oca ña Amelia Farr és Source Type: research

Recycling selectable markers via Cre/loxP system for constructing Komagataella phaffii strains co-expressing multiple proteins
CONCLUSIONS: With easy manipulation, the method was effective in recycling of the selectable markers, and consequently two protein genes were sequential integrated chromosomally and successfully co-expressed in the yeast.PMID:38416308 | DOI:10.1007/s10529-024-03466-3 (Source: Biotechnology Letters)
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Weixian Wang Minghai Han Guofei Zhu Xiaohui Liu Tianming Zhao Xiaoyan Ma Xun Gong Cunbin Xu Source Type: research

ANCUT1, a novel thermoalkaline cutinase from Aspergillus nidulans and its application on hydroxycinnamic acids lipophilization
Biotechnol Lett. 2024 Feb 28. doi: 10.1007/s10529-024-03467-2. Online ahead of print.ABSTRACTOne of the four cutinases encoded in the Aspergillus nidulans genome, ANCUT1, is described here. Culture conditions were evaluated, and it was found that this enzyme is produced only when cutin is present in the culture medium, unlike the previously described ANCUT2, with which it shares 62% amino acid identity. The differences between them include the fact that ANCUT1 is a smaller enzyme, with experimental molecular weight and pI values of 22 kDa and 6, respectively. It shows maximum activity at pH 9 and 60 °C under assayed condi...
Source: Biotechnology Letters - February 28, 2024 Category: Biotechnology Authors: Carolina Pe ña-Montes Eva Berm údez-García Denise Castro-Ochoa Fernanda Vega-P érez Katia Esqueda-Dom ínguez Jos é Augusto Castro-Rodríguez Augusto Gonz ález-Canto Laura Segoviano-Reyes Arturo Navarro-Oca ña Amelia Farr és Source Type: research