Results 81 to 90 of about 13,570,727 (154)

Safety evaluation of the food enzyme β‐glucanase, xylanase and cellulase from Mycothermus thermophiloides (strain NZYM‐ST)

EFSA Journal, 2019
The food enzyme has three declared activities (endo‐1,3(4)‐β‐glucanase EC 3.2.1.6, endo‐1,4‐β‐xylanase EC 3.2.1.8 and cellulase (endo‐1,4‐β‐d‐glucanase EC 3.2.1.4)) and is produced with a non‐genetically modified Mycothermus thermophiloides strain by ...
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (EFSA CEP Panel), Vittorio Silano, José Manuel Barat Baviera, Claudia Bolognesi, Beat Johannes Brüschweiler, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Evgenia Lampi, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk Van Loveren, Laurence Vernis, Holger Zorn, Boet Glandorf, Francesca Marcon, André Penninks, Jaime Aguilera, Magdalena Andryszkiewicz, Davide Arcella, Joaquim Maia, Yi Liu, Andrew Chesson   +25 more
doaj   +1 more source

Characterization of thermophilic fungi producing extracellular lignocellulolytic enzymes for lignocellulosic hydrolysis under solid-state fermentation

Bioresources and Bioprocessing, 2018
Background Thermotolerant lignocellulolytic enzymes have become a subject of interest in industrial processes due to their ability to degrade lignocellulosic polysaccharides.
Paramjeet Saroj, Manasa P, Korrapati Narasimhulu   +2 more
doaj   +1 more source

Safety evaluation of the food enzyme containing endo‐polygalacturonase, pectinesterase, pectin lyase and arabinan endo‐1,5‐α‐l‐arabinanase activities from the non‐genetically modified Aspergillus sp. strain ASNSC

EFSA Journal, Volume 24, Issue 10, October 2026.
Abstract The food enzyme containing endo‐polygalacturonase (1,4‐α‐d‐galacturonan glycanohydrolase; EC 3.2.1.15), pectinesterase (pectin pectylhydrolase; EC 3.1.1.11), pectin lyase (1,4‐6‐O‐methyl‐α‐d‐galacturonan lyase; EC 4.2.2.10) and arabinan endo‐1,5‐α‐l‐arabinanase (5‐α‐l‐arabinan 5‐α‐l‐arabinanohydrolase; EC 3.2.1.99) activities is produced with ...
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, Cristina Andreoli, Andrea Terron, Andrey Yurkov, Magdalena Andryszkiewicz, Daniele Cavanna, Ana Criado, Simone Lunardi, Yi Liu   +20 more
wiley   +1 more source

Purification and biochemical Properties of xylanase from

, 2009
[[abstract]]Xylooligosaccharides, such as xylobiose and xylotriose, have been considered as a potential health food. They can be produced by digesting hemicellulose with xylanase.
Po-Yao Wang
core  

Exploiting endo-β-1, 4-xylanase enzyme from fungal origin for green leather processing: A novel and sustainable strategy

, 2021
The linear polysaccharide β-1, 4-xylan (hemicellulose), one of the major components of plant cell walls, is considered as by product in paper making process.
Kausik Majumder, Ivy Kanungo, Debosmita Sikdar   +2 more
core   +1 more source

Safety evaluation of an extension of use of the food enzyme non‐reducing end α‐l‐arabinofuranosidase from the genetically modified Trichoderma reesei strain NZYM‐GV

EFSA Journal, Volume 24, Issue 10, October 2026.
Abstract The food enzyme non‐reducing end α‐l‐arabinofuranosidase (α‐l‐arabinofuranoside non‐reducing end α‐l‐arabinofuranosidase; EC 3.2.1.55) is produced with the genetically modified Trichoderma reesei strain NZYM‐GV by Novozymes A/S. The safety of this food enzyme was evaluated previously, and it did not give rise to safety concerns when used in ...
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, Daniele Cavanna, Yi Liu, Valentina Tokić   +15 more
wiley   +1 more source

Co-immobilization and stabilization of xylanase, β-xylosidase and α-L-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis [PDF]

, 2016
Differently activated agarose-based supports were evaluated for co-immobilization of a crude extract from Penicillium janczewskii containing xylanase, β-xylosidase and α-l-arabinofuranosidase activities.
Cano Carmona, Eleonora, Carmona, Eleonora Cano, Moreno-Pérez, Sonia, Pessela, Benevides Costa, Guisán, José Manuel, Carmona, Eleonora Cano [UNESP], Fanchini Terrasan, César Rafael, Trobo-Maseda, Lara, Pessela, Benevides C.   +8 more
core   +1 more source

The Mechanisms of Catalysis by Metallo β-Lactamases [PDF]

, 2008
Class B β-lactamases or metallo-β-lactamases (MBLs) require zinc ions to catalyse the hydrolysis of β-lactam antibiotics such as penicillins, cephalosporins, carbapenems, and cephamycins.
Michael I. Page, Page, Michael I., Badarau, Adriana, Adriana Badarau   +3 more
core   +3 more sources

Safety and efficacy of Amylofeed® (endo‐1,3(4)‐β‐glucanase and endo‐1,4‐β‐xylanase and α‐amylase) as a feed additive for piglets and minor growing porcine species

EFSA Journal, 2018
Amylofeed® is a feed additive that contains glucanase, xylanase and amylase activities, and it is intended to be used as a zootechnical additive for weaned piglets and minor porcine species. In previous assessments, the additive was characterised and the
EFSA Panel on Additives and Products or Substances used in Animal Feed (EFSA FEEDAP Panel), Guido Rychen, Gabriele Aquilina, Giovanna Azimonti, Vasileios Bampidis, Maria de Lourdes Bastos, Georges Bories, Andrew Chesson, Pier Sandro Cocconcelli, Gerhard Flachowsky, Jürgen Gropp, Boris Kolar, Maryline Kouba, Marta López‐Alonso, Secundino López Puente, Alberto Mantovani, Baltasar Mayo, Fernando Ramos, Maria Saarela, Roberto Edoardo Villa, Robert John Wallace, Pieter Wester, Paul Brantom, Noël Dierick, Montserrat Anguita   +24 more
doaj   +1 more source

Characterization of a xylanase inhibitor TAXI-I from wheat

, 2010
Xylanase inhibitor TAXI-I gene was cloned from wheat (Triticum aestivum L.) and then TAXI-I encoding sequence was expressed in Escherichia coli. The recombinant TAXI-I protein inhibited glycoside hydrolase (GH) family 11 xylanases in Aspergillus niger ...
X. -Y. Weng, Y. -Y. Huang, J. -Y. Sun, H. Gao   +3 more
core   +1 more source