Results 31 to 40 of about 1,366 (148)

Safety evaluation of the food enzyme α‐amylase from the genetically modified Bacillus licheniformis strain DP‐Dzb45

EFSA Journal, 2020
The food enzyme α‐amylase (1,4‐α‐D‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the genetically modified Bacillus licheniformis strain DP‐Dzb45 by Danisco US Inc.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Vittorio Silano, José Manuel Barat Baviera, Claudia Bolognesi, Pier Sandro Cocconcelli, Riccardo Crebelli, David Michael Gott, Konrad Grob, Claude Lambré, Evgenia Lampi, Marcel Mengelers, Alicja Mortensen, Gilles Rivière, Inger‐Lise Steffensen, Christina Tlustos, Henk van Loveren, Laurence Vernis, Holger Zorn, Boet Glandorf, Lieve Herman, Magdalena Andryszkiewicz, Ana Gomes, Natália Kovalkovičová, Yi Liu, Joaquim Maia, Andrew Chesson   +25 more
doaj   +1 more source

Random mutagenesis and process optimization of bacterial co-culture for hyperproduction of 1, 4-α-D-glucan glucanohydrolase using submerged fermentation

, 2018
The exponential increase in the application of 1,4-α-D-glucan glucanohydrolase (GGH) in various fields has placed stress and demand in both qualitative improvement and quantitative enhancement through strain improvement.
R. Abdullah, Samra Kiran, M. Iqtedar, A. Kaleem, F. Saleem, T. Iftikhar, J. S. Cheema, S. Naz   +7 more
semanticscholar   +1 more source

Characterization of Nitric Oxide Modulatory Activities of Alkaline-Extracted and Enzymatic-Modified Arabinoxylans from Corn Bran in Cultured Human Monocytes [PDF]

, 2016
This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Agricultural and Food Chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher.
Ashworth, Jason J., Li, Weili, Smith, Christopher J., Zhang, Zhengxiao   +3 more
core   +2 more sources

Densely packed matrices as rate determining features in starch hydrolysis [PDF]

, 2015
To aid in the design of starch-containing foods with slow and/or incomplete digestion in the upper gastrointestinal tract, the starch structural factors which control the rate of action of alpha-amylase are reviewed.
Dhital, Sushil, Gidley, Michael J, Zhang, Bin   +2 more
core   +1 more source

Lignocellulose biotechnology: issues of bioconversion and enzyme production [PDF]

, 2004
This review is written from the perspective of scientists working in lignocellulose bioconversion in a developing country and the aim of this review is to remind ourselves and other scientists working in related areas of lignocellulose research of the ...
Abotsi, E, Howard, RL, Howard, S, Jansen van Rensburg, EL   +3 more
core   +2 more sources

Beta-glucans from biomass of plant and microbial origin [PDF]

, 2019
The aim of the present study is to explore the transformation of (1→3)(1→4)-β-D-glucans of rye biomass by Aspergills niger and accumulation of (1→3)(1→6)-β-D-glucans in the microbial cell wall.Biomass from rye grain was obtained as a result of enzymatic ...
A. Printseva A., B. Manzhieva S., B. Manzhieva S., N. Sharova Yu., N. Sharova Yu., T. Vybornova V., T. Vybornova V., А. Printseva А.   +7 more
core   +4 more sources

Safety evaluation of the food enzyme α‐amylase from a genetically modified Aspergillus niger (strain NZYM‐MC)

EFSA Journal, 2018
The food enzyme alpha‐amylase (4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the genetically modified strain of Aspergillus niger by Novozymes A/S. The genetic modifications do not give rise to safety concerns.
EFSA Panel on Food Contact Materials, Enzymes, Processing Aids (CEP), 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 Riviere, Inger‐Lise Steffensen, Christina Tlustos, Henk van Loveren, Laurence Vernis, Holger Zorn, Sirpa Kärenlampi, Francesca Marcon, André Penninks, Andrew Smith, Margarita Aguilera‐Gómez, Magdalena Andryszkiewicz, Davide Arcella, Natália Kovalkovičová, Yi Liu, Annamaria Rossi, Karl‐Heinz Engel, Andrew Chesson   +28 more
doaj   +1 more source

Safety evaluation of the food enzyme alpha‐amylase from a genetically modified Bacillus subtilis (strain NBA)

EFSA Journal, 2019
The food enzyme alpha‐amylase (4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with a genetically modified strain of Bacillus subtilis strain NBA by DSM Food Specialities B.V. This α‐amylase is intended to be used in baking processes.
EFSA Panel on Food Contact Materials, Enzymes, Processing Aids (CEP), 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, Lieve Herman, André Penninks, Davor Želježic, Magdalena Andryszkiewicz, Davide Arcella, Yi Liu, Karl‐Heinz Engel, Andrew Chesson   +24 more
doaj   +1 more source

Safety evaluation of the food enzyme α‐amylase from the genetically modified Pseudomonas fluorescens strain BD15754

EFSA Journal, 2020
The food enzyme α‐amylase (4‐a‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the genetically modified Pseudomonas fluorescens strain BD15754 by BASF Enzymes LLC1.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), Vittorio Silano, José Manuel Barat Baviera, Claudia Bolognesi, 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, Lieve Herman, Jaime Aguilera, Magdalena Andryszkiewicz, Yi Liu, Andrew Chesson   +21 more
doaj   +1 more source

From carbohydrates to drug-like fragments: Rational development of novel [alfa]-amylase inhibitors [PDF]

, 2018
K
Al,-Asri, Jamil, Fazekas, Erika, Gyémánt, Gyöngyi, Görick, Cornelia, Lehoczki, Gábor, Melzig, Matthias F., Mortier, Jérémie, Perdih, Andrej, Wolber, Gerhard   +8 more
core   +1 more source