Safety evaluation of the food enzyme containing endo-1,3(4)-β-glucanase, endo-1,4-β-xylanase and cellulase activities from the non-genetically modified <i>Rasamsonia emersonii</i> strain FGB. [PDF]
Abstract The food enzyme containing endo‐1,3(4)‐β‐glucanase (3‐(1,3;1,4)‐β‐d‐glucan 3(4)‐glucanohydrolase; EC 3.2.1.6), endo‐1,4‐β‐xylanase (4‐β‐d‐xylan xylanohydrolase; EC 3.2.1.8) and cellulase (4‐(1,3;1,4)‐β‐d‐glucan‐4‐glucanohydrolase EC 3.2.1.4) is produced with the non‐genetically modified Rasamsonia emersonii strain FGB by DSM Food Specialties B.
EFSA Panel on Food Enzymes (FEZ) +18 more
europepmc +2 more sources
Aims: Here, we describe a novel way to produce an endo-1,4-beta-xylanase from Aspergillus clavatus using paper and pulp industry waste. Methodology: Optimal Aspergillus clavatus NRRL1 cultivation conditions were evaluated using minimal medium with different concentrations (1 to 10%) of paper sludge pretreated with HCl, during different periods ...
Maria de Lourdes T. M. Polizeli +5 more
openaire +2 more sources
Probe-mining of endo-1,4-beta-xylanase from goats-rumen bacterial metagenomic DNA data
Endo-1,4-beta-xylanases (xylanases) are classified into 9 glycoside hydrolase families, GH5, 8, 10, 11, 30, 43, 51, 98, and 141 based on the CAZy database. The probe sequences representing the enzymes were constructed from published sequences of actual experimental studies with xylan decomposition activity.
Dao Trong Khoa +2 more
openaire +2 more sources
Aspects microbiologiques de la production par fermentation solide des endo-beta-1,4-xylanases de moisissures : le cas de Penicillium canescens [PDF]
Microbial aspects of endo-β-1,4-xylanase production in solid-state fermentation by Penicillia: the case of Penicillium canescens. Production of xylanases by Penicillium canescens 10-10c is the research object in Walloon Center of Industrial Biology ...
Assamoi AA., Destain J., Thonart P.
doaj
Computational design of an endo-1,4- -xylanase ligand binding site [PDF]
The field of computational protein design has experienced important recent success. However, the de novo computational design of high-affinity protein-ligand interfaces is still largely an open challenge. Using the Rosetta program, we attempted the in silico design of a high-affinity protein interface to a small peptide ligand.
Andrew, Morin +5 more
openaire +2 more sources
The biochemical properties of a purified enzyme of a new alkalophillic endo-1,4-beta-xylanase gene, KRICT PX2 (GU967374), which was isolated from Paenibacillus sp. HPL-002 (KCTC11410BP) and expressed in E. coli, were investigated. The specific activity of the purified xylanase was 51.26 μmol/min/mg proteins.
No-Joong Park, +5 more
openaire +2 more sources
Safety and efficacy of Hostazym® X (endo‐1,4‐beta‐xylanase) as a feed additive for sows in order to have benefit in piglets [PDF]
Following a request from the European Commission, the Panel on Additives and Products or Substances used in Animal Feed (FEEDAP) was asked to deliver a scientific opinion on the safety and efficacy of HOSTAZYM ® X as a feed additive for sows in order to have benefit in piglets.
EFSA Panel on Additives and Products or Substances used in Animal Feed (EFSA FEEDAP Panel) +22 more
openaire +3 more sources
Three‐dimensional structure of endo‐1,4‐beta‐xylanase II from Trichoderma reesei: two conformational states in the active site. [PDF]
The three-dimensional structure of endo-1,4-beta-xylanase II (XYNII) from Trichoderma reesei has been determined by X-ray diffraction techniques and refined to a conventional R-factor of 18.3% at 1.8 A resolution. The 190 amino acid length protein was found to exist as a single domain where the main chain folds to form two mostly antiparallel beta ...
A, Törrönen, A, Harkki, J, Rouvinen
openaire +2 more sources
Abstract The search for sustainable alternatives for bioethanol production has encouraged the valorization of agro‐industrial residues. This study evaluated the use of residual barley as a feedstock for bioethanol production and as a potential ingredient for ruminant feed.
Gabrielle Fusiger Berwian +4 more
wiley +1 more source
This review highlights non‐thermal extraction technologies for seaweed proteins, emphasizing their mechanisms, impacts on protein structure and functionality, and sustainability potential. Key limitations related to species dependence, extract complexity, and scale‐up are discussed to guide future industrial and biorefinery applications.
Rahat Mahmud +3 more
wiley +1 more source

