Results 91 to 100 of about 15,587 (221)

Safety evaluation of the food enzyme endo‐1,4‐β‐xylanase from the genetically modified Bacillus licheniformis strain NZYM‐FX

open access: yesEFSA Journal, Volume 24, Issue 5, May 2026.
Abstract The food enzyme endo‐1,4‐β‐xylanase (4‐β‐d‐xylan xylanohydrolase; EC 3.2.1.8) is produced with the genetically modified Bacillus licheniformis strain NZYM‐FX by Novozymes A/S. The production strain meets the requirements for the qualified presumption of safety (QPS) approach.
EFSA Panel on Food Enzymes (FEZ)   +15 more
wiley   +1 more source

Digestibilidad in situ de dietas con harina de nopal deshidratado conteniendo un preparado de enzimas fibrolíticas exógenas In situ digestibility in dehydrated ground prickly pear diets containing a fybrolitic enzymes product

open access: yesPesquisa Agropecuária Brasileira, 2006
Se evaluó el efecto de un preparado de enzimas fibrolíticas exógenas (celulasas y xilanasas) en la degradabilidad in situ de la materia seca (DisMS), fibra detergente neutro (DFDNr) y fibra detergente ácido residual (DFDAr), en dietas altas o bajas en ...
Marco Medina Romo   +4 more
doaj   +1 more source

A Symbiont-Independent Endo-1,4-β-Xylanase from the Plant-Parasitic Nematode Meloidogyne incognita [PDF]

open access: yes, 2006
Substituted xylan polymers constitute a major part of the hemicellulose fraction of plant cell walls, especially in monocotyledons. Endo-1,4-β-xylanases (EC 3.2.1.8) are capable of hydrolyzing substituted xylan polymers into fragments of random size ...
Bakker, Jaap   +6 more
core  

Optimization of fermentation media and growth conditions for microbial xylanase production [PDF]

open access: yes, 2016
Efficiency of cellulase-free xylanases is one of the determining factors in paper and pulp industries. Use of microbes which can produce cellulase-free xylanases may help to overcome the current challenges in kraft pulp processing.
Bushra Kalim, Nazish Mazhar Ali
core   +1 more source

Safety evaluation of an extension of use of the food enzyme endo‐1,4‐β‐xylanase from the genetically modified Bacillus licheniformis strain NZYM‐FX

open access: yesEFSA Journal, Volume 24, Issue 5, May 2026.
Abstract The food enzyme endo‐1,4‐β‐xylanase (4‐β‐d‐xylan xylanohydrolase; EC 3.2.1.8) is produced with the genetically modified Bacillus licheniformis strain NZYM‐FX 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 two food manufacturing processes.
EFSA Panel on Food Enzymes (FEZ)   +14 more
wiley   +1 more source

.BETA.-1,3-Xylanase and .BETA.-1,4-xylanase action on rhodymenan.

open access: yesAgricultural and Biological Chemistry, 1986
A purified extracellular endo β-1, 3-xylanase (EC 3.2.1.32) from an isolated strain, Aspergillus reus A-07, was found to hydrolyze 1, 3-xylosyl linkages only. When rhodymenan (β-1, 4 and β-1, 3-linked xylan) was hydrolyzed by β-1, 3-xylanase (EF-6), four β-1, 4-linked xylooligosaccharide ictions were produced.
Wen Pin CHEN   +2 more
openaire   +2 more sources

Scavenging Activity of Enzymatic Hydrolysates from Wheat Bran

open access: yesFood Technology and Biotechnology, 2009
Wheat bran was destarched and deproteinated by α-amylase, protease and amyloglucosidase successively, and further hydrolyzed using Bacillus subtilis xylanases. The yield of enzymatic hydrolysates from wheat bran (EHWB) was 1.84 %.
Jing Wang   +4 more
doaj  

Cloning of novel bacterial xylanases from lignocellulose-enriched compost metagenomic libraries

open access: yesAMB Express, 2019
Xylanases are in important class of industrial enzymes that are essential for the complete hydrolysis of lignocellulosic biomass into fermentable sugars.
Simo Ellilä   +6 more
doaj   +1 more source

A glucuronoxylan-specific xylanase from a new Paenibacillus favisporus strain isolated from tropical soil of Brazil [PDF]

open access: yes, 2015
A new xylanolytic strain, Paenibacillus favisporus CC02-N2, was isolated from sugarcane plantation fi elds in Brazil. The strain had a xylan-degrading system with multiple enzymes, one of which, xylanase Xyn30A, was identifi ed and characterized.
Demetrius A.M. de Araújo   +5 more
core   +1 more source

Improvement of β‐Xylosidase and Endoxylanase Activities in Talaromyces amestolkiae by Genetic Manipulation of the Transcriptional Activator XlnR

open access: yesMicrobial Biotechnology
The ascomycete Talaromyces amestolkiae is a promising source of glycosyl hydrolases for hemicellulose degradation, as it contains a considerably higher number of genes encoding these enzymes than other fungi exploited for plant biomass valorisation.
Ana Pozo‐Rodríguez   +4 more
doaj   +1 more source

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