Niklas Broel
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Niklas Broel has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
- Alexander Siegl
Optiferm GmbH, 87466 Oy-Mittelberg, Germany
1 shared publication - Binglin Li
College of Food Science and Engineering, Northwest University, Xi'an 710069, China
1 shared publication - Edgar Weichhard
Optiferm GmbH, 87466 Oy-Mittelberg, Germany
1 shared publication - Holger Zorn
Institute of Food Chemistry and Food Biotechnology, University of Giessen, Giessen, Germany
1 shared publication - Julia Manhard
Optiferm GmbH, 87466 Oy-Mittelberg, Germany
1 shared publication - Martin Gand
Institute of Food Chemistry and Food Biotechnology, Justus Liebig University Giessen, Heinrich-Buff-Ring 17, Giessen 35392, Germany
1 shared publication
Latest Publications
- Open Access
Altering the Chain Length Specificity of a Lipase from Pleurotus citrinopileatus for the Application in Cheese Making
In traditional cheese making, pregastric lipolytic enzymes of animal origin are used for the acceleration of ripening and the formation of spicy flavor compounds. Especially for cheese specialities, such as Pecorino, Provolone, or Feta, pregastric esterases (PGE) play an important role. A lipase from Pleurotus citrinopileatus could serve as a substitute for these animal-derived enzymes, thus offering vegetarian, kosher, and halal alternatives. However, the hydrolytic activity of this enzyme towards long-chain fatty acids is slightly too high, which may lead to off-flavors during long-term ripening. Therefore, an optimization via protein engineering (PE) was performed by changing the specificity towards medium-chain fatty acids. With a semi-rational design, possible mutants at eight different positions were created and analyzed in silico. Heterologous expression was performed for 24 predicted mutants, of which 18 caused a change in the hydrolysis profile. Three mutants (F91L, L302G, and L305A) were used in application tests to produce Feta-type brine cheese. The sensory analyses showed promising results for cheeses prepared with the L305A mutant, and SPME-GC-MS analysis of volatile free fatty acids supported these findings. Therefore, altering the chain length specificity via PE becomes a powerful tool for the replacement of PGEs in cheese making.
Open AccessAltering the Chain Length Specificity of a Lipase from Pleurotus citrinopileatus for the Application in Cheese Making
In traditional cheese making, pregastric lipolytic enzymes of animal origin are used for the acceleration of ripening and the formation of spicy flavor compounds. Especially for cheese specialities, such as Pecorino, Provolone, or Feta, pregastric esterases (PGE) play an important role. A lipase from Pleurotus citrinopileatus could serve as a substitute for these animal-derived enzymes, thus offering vegetarian, kosher, and halal alternatives. However, the hydrolytic activity of this enzyme towards long-chain fatty acids is slightly too high, which may lead to off-flavors during long-term ripening. Therefore, an optimization via protein engineering (PE) was performed by changing the specificity towards medium-chain fatty acids. With a semi-rational design, possible mutants at eight different positions were created and analyzed in silico. Heterologous expression was performed for 24 predicted mutants, of which 18 caused a change in the hydrolysis profile. Three mutants (F91L, L302G, and L305A) were used in application tests to produce Feta-type brine cheese. The sensory analyses showed promising results for cheeses prepared with the L305A mutant, and SPME-GC-MS analysis of volatile free fatty acids supported these findings. Therefore, altering the chain length specificity via PE becomes a powerful tool for the replacement of PGEs in cheese making.