Results 1 to 10 of about 2,670 (168)

Safety evaluation of an extension of use of the food enzyme pectinesterase from the genetically modified Trichoderma reesei strain RF6201 [PDF]

EFSA Journal
The food enzyme pectinesterase (pectin pectylhydrolase, EC 3.1.1.11) is produced with the genetically modified Trichoderma reesei strain RF6201 by AB Enzymes GmbH.
EFSA Panel on Food Enzymes (FEZ), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L. M. Solano, Monika Sramkova, Henk Van Loveren, Laurence Vernis, Jeroen Pasch, Yi Liu   +15 more
doaj   +2 more sources

Genome-Wide Association Study of Plant and Ear Height in Maize (Zea mays L.) and Identification of Candidate Genes [PDF]

Plants
Maize is one of the most widely cultivated crops worldwide and is extensively used for animal feed and industrial applications. Plant height (PH) and ear height (EH) are critical determinants of lodging resistance and tolerance to high planting density ...
Jiahao Wang, Yujia Zhang, Xinping Guo, Hexuan Liu, Liangliang Bao, Yuyang Zhou, Chunxiang Li, Hong Di   +7 more
doaj   +2 more sources

Safety evaluation of the food enzyme pectinesterase from the genetically modified Trichoderma reesei strain RF6201 [PDF]

EFSA Journal, 2023
The food enzyme pectinesterase (pectin pectylhydrolase; EC 3.1.1.11) is produced with the genetically modified Trichoderma reesei strain RF6201 by AB Enzymes GmbH. The genetic modifications do not give rise to safety concerns.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Boet Glandorf, Magdalena Andryszkiewicz, Ana Gomes, Natalia Kovalkovicova, Yi Liu, Giulio diPiazza, Andrew Chesson   +23 more
doaj   +2 more sources

Safety evaluation of the food enzyme pectinesterase from the genetically modified Aspergillus niger strain PME [PDF]

EFSA Journal, 2023
The food enzyme pectinesterase (pectin pectylhydrolase; EC 3.1.1.11) is produced with the genetically modified Aspergillus niger strain PME by DSM Food Specialties B.V. The genetic modifications do not give rise to safety concerns.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Claude Lambré, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Lieve Herman, Jaime Aguilera, Magdalena Andryszkiewicz, Rita Ferreira deSousa, Yi Liu, Sandra Rainieri, Andrew Chesson   +23 more
doaj   +2 more sources

Crystal Structure of the Multidomain Pectin Methylesterase PmeC5 from Butyrivibrio fibrisolvens D1^T [PDF]

Biomolecules
Pectin is a dynamic and complex polysaccharide that forms a substantial proportion of the primary plant cell wall and middle lamella of forage ingested by grazing ruminants.
Vincenzo Carbone, Kerri Reilly, Carrie Sang, Linley R. Schofield, William J. Kelly, Ron S. Ronimus, Graeme T. Attwood, Nikola Palevich   +7 more
doaj   +2 more sources

Safety evaluation of the food enzyme pectinesterase from the non‐genetically modified Aspergillus luchuensis strain CBS 148463 [PDF]

EFSA Journal
The food enzyme pectinesterase (pectin pectylhydrolase; EC 3.1.1.11) is produced with the non‐genetically modified Aspergillus luchuensis strain CBS 148463 by Solyve. The food enzyme was considered free from viable cells of the production organism.
EFSA Panel on Food Enzymes (FEZ), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L. M. Solano, Henk Van Loveren, Laurence Vernis, Jaime Aguilera, Magdalena Andryszkiewicz, Ana Criado, Francesco Pesce, Yi Liu   +17 more
doaj   +2 more sources

Pectinesterase activity and gene expression correlate with pathogenesis of Phytophthora infestans [PDF]

Frontiers in Plant Science
Late blight caused by Phytophthora infestans is the most devastating disease of potato. Phytophthora infestans produces many secondary metabolites and effector proteins, involved in the pathogenesis, which compromise host defense mechanisms ...
Linmei Deng, Xun Huang, Jian Dao, Yajin Xu, Kunyan Zhou, Wenping Wang, Chunjiang Liu, Meng Chen, Shunhong Zhang, Yue Zhang, Jianjun Hao, Xia Liu, Yanli Yang   +12 more
doaj   +2 more sources

Integrated Transcriptome and Proteome Analysis Reveals That Cell Wall Activity Affects Phelipanche aegyptiaca Parasitism [PDF]

Plants
Phelipanche aegyptiaca can infect many crops, causing large agricultural production losses. It is important to study the parasitism mechanism of P. aegyptiaca to control its harm. In this experiment, the P.
Meixiu Chen, Lu Zhang, Zhaoqun Yao, Xiaolei Cao, Qianqian Ma, Siyu Chen, Xuekun Zhang, Sifeng Zhao   +7 more
doaj   +2 more sources

Chemical Composition, Functional and Antioxidant Properties of Dietary Fibre Extracted from Lemon Peel after Enzymatic Treatment [PDF]

Molecules
Lemon peel represents an interesting by-product owing to its content of dietary fibre (DF) and (poly)phenols, which is of great importance for its valorisation.
Vanesa Núñez-Gómez, Marta San Mateo, Rocío González-Barrio, Mª Jesús Periago   +3 more
doaj   +2 more sources

Purification and properties of pectinesterase from papaya

Journal of the Science of Food and Agriculture, 1984
AbstractPectinesterase (PE) was partially purified from papaya pulp, and its biochemical properties were studied. The enzyme was eluted in a single peak after DEAE‐cellulose and Sephadex G‐100 chromatography. The PE had a molecular weight of 53000 and showed an optimum pH of 8.0. Its activity was dependent on an NaCl concentration of 0.2M.
Lourenco, Euclides J., Catutani, Adelaide T.   +1 more
exaly   +3 more sources