Results 31 to 40 of about 537 (137)

Image_2_The journey of cardosin A in young Arabidopsis seedlings leads to evidence of a Golgi-independent pathway to the protein storage vacuole.tiff

, 2023
The aspartic proteinase cardosin A is a vacuolar enzyme found to accumulate in protein storage and lytic vacuoles in the flowers and protein bodies in the seeds of the native plant cardoon.
Vanessa Vieira (9308036), José Pissarra (16506843), Cláudia Pereira (4861405), Susana Pereira (2686432)   +3 more
core   +1 more source

Image_5_The journey of cardosin A in young Arabidopsis seedlings leads to evidence of a Golgi-independent pathway to the protein storage vacuole.tiff

, 2023
The aspartic proteinase cardosin A is a vacuolar enzyme found to accumulate in protein storage and lytic vacuoles in the flowers and protein bodies in the seeds of the native plant cardoon.
Vanessa Vieira (9308036), José Pissarra (16506843), Cláudia Pereira (4861405), Susana Pereira (2686432)   +3 more
core   +1 more source

Image_1_The journey of cardosin A in young Arabidopsis seedlings leads to evidence of a Golgi-independent pathway to the protein storage vacuole.tiff

, 2023
The aspartic proteinase cardosin A is a vacuolar enzyme found to accumulate in protein storage and lytic vacuoles in the flowers and protein bodies in the seeds of the native plant cardoon.
Vanessa Vieira (9308036), José Pissarra (16506843), Cláudia Pereira (4861405), Susana Pereira (2686432)   +3 more
core   +1 more source

Image_6_The journey of cardosin A in young Arabidopsis seedlings leads to evidence of a Golgi-independent pathway to the protein storage vacuole.tif

, 2023
The aspartic proteinase cardosin A is a vacuolar enzyme found to accumulate in protein storage and lytic vacuoles in the flowers and protein bodies in the seeds of the native plant cardoon.
Vanessa Vieira (9308036), José Pissarra (16506843), Cláudia Pereira (4861405), Susana Pereira (2686432)   +3 more
core   +1 more source

Image_4_The journey of cardosin A in young Arabidopsis seedlings leads to evidence of a Golgi-independent pathway to the protein storage vacuole.tiff

, 2023
The aspartic proteinase cardosin A is a vacuolar enzyme found to accumulate in protein storage and lytic vacuoles in the flowers and protein bodies in the seeds of the native plant cardoon.
Vanessa Vieira (9308036), José Pissarra (16506843), Cláudia Pereira (4861405), Susana Pereira (2686432)   +3 more
core   +1 more source

Image_7_The journey of cardosin A in young Arabidopsis seedlings leads to evidence of a Golgi-independent pathway to the protein storage vacuole.tif

, 2023
The aspartic proteinase cardosin A is a vacuolar enzyme found to accumulate in protein storage and lytic vacuoles in the flowers and protein bodies in the seeds of the native plant cardoon.
Vanessa Vieira (9308036), José Pissarra (16506843), Cláudia Pereira (4861405), Susana Pereira (2686432)   +3 more
core   +1 more source

The Role of Microbial Aspartic Protease Enzyme in Food and Beverage Industries

Journal of Food Quality, Volume 2018, Issue 1, 2018., 2018
Proteases represent one of the three largest groups of industrial enzymes and account for about 60% of the total global enzymes sale. According to the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, proteases are classified in enzymes of class 3, the hydrolases, and the subclass 3.4, the peptide hydrolases or ...
Jermen Mamo, Fassil Assefa, Antimo Di Maro   +2 more
wiley   +1 more source

Image_3_The journey of cardosin A in young Arabidopsis seedlings leads to evidence of a Golgi-independent pathway to the protein storage vacuole.tiff

, 2023
The aspartic proteinase cardosin A is a vacuolar enzyme found to accumulate in protein storage and lytic vacuoles in the flowers and protein bodies in the seeds of the native plant cardoon.
Vanessa Vieira (9308036), José Pissarra (16506843), Cláudia Pereira (4861405), Susana Pereira (2686432)   +3 more
core   +1 more source

Functional Characterization of the N‐Terminal C2 Domain from Arabidopsis thaliana Phospholipase Dα and Dβ

BioMed Research International, Volume 2016, Issue 1, 2016., 2016
Most of plant phospholipases D (PLD) exhibit a C2‐lipid binding domain of around 130 amino acid residues at their N‐terminal region, involved in their Ca2+‐dependent membrane binding. In this study, we expressed and partially purified catalytically active PLDα from Arabidopsis thaliana (AtPLDα) in the yeast Pichia pastoris.
Renaud Rahier, Alexandre Noiriel, Abdelkarim Abousalham, Pengjun Shi   +3 more
wiley   +1 more source

Protease from Aspergillus oryzae: Biochemical Characterization and Application as a Potential Biocatalyst for Production of Protein Hydrolysates with Antioxidant Activities

Journal of Food Processing, Volume 2014, Issue 1, 2014., 2014
This study reports the biochemical characterization of a protease from Aspergillus oryzae LBA 01 and the study of the antioxidant properties of protein hydrolysates produced with this protease. The biochemical characterization showed that the enzyme was most active over the pH range 5.0–5.5 and was stable from pH 4.5 to 5.5.
Ruann Janser Soares de Castro, Helia Harumi Sato, Harshadrai M. Rawel   +2 more
wiley   +1 more source