Results 21 to 30 of about 968 (115)

Safety evaluation of the food enzyme glucan‐1,4‐α‐glucosidase from the non‐genetically modified Rhizopus delemar strain CU634‐1775

EFSA Journal, 2023
The food enzyme glucan‐1,4‐α‐glucosidase (4‐α‐d‐glucan glucohydrolase; EC 3.1.2.3) is produced with the non‐genetically modified Rhizopus delemar strain CU634‐1775 by Shin Nihon Chemical Co., Ltd.
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, Jaime Aguilera, Magdalena Andryszkiewicz, Natalia Kovalkovicova, Yi Liu, Giulio diPiazza, Rita deFerreira de Sousa, Andrew Chesson   +24 more
doaj   +1 more source

Effect of enzymatic treatment of different starch sources on the in vitro rate and extent of starch digestion:[plus] Correction [PDF]

, 2012
Gelatinized wheat, potato and waxy maize starches were treated enzymatically in order to increase the degree of branching of the amylopectin fraction and thereby change the starch degradation profile towards a higher proportion of slowly digestible ...
Larsen, Flemming Hofmann, Mirosław Marek Kasprzak, Helle Nygaard Lærke, Pedersen, Sven, Sven Pedersen, Jørgensen, Anne Skov, Anne Skov Jørgensen, Lærke, Helle Nygaard, Knudsen, Knud Erik Bach, Flemming Hofmann Larsen, Knud Erik Bach Knudsen, Kasprzak, Miroslaw Marek   +11 more
core   +1 more source

A Kinetic Model for Cassava Starch Hydrolysis under Cold Enzyme Two-Stage Hydrolysis Condition [PDF]

, 2011
A suitable starch hydrolysis strategy is crucial for conversion of starch into fermentable sugar, both with regard to reducing hydrolysis cost and increasing hydrolysis efficiency.
Zong Cheng Yan, Li Chen, Hong Lin Wang, Ying Ling Bao   +3 more
core   +1 more source

Synthesis of 2-O-a-D-glucopyranosyl L-ascorbic acid by cyclomaltodextrin glucanotransferase from bacillus sp. [PDF]

, 2006
Cyclomaltodextrin glucanotransferase (CGTase) [EC 2.4.1.19] was found to catalyze the transglycosylation from α-cyclodextrin (α-CD) to l-ascorbic acid (AA).
Abd. Rahman, Roshanida
core   +1 more source

Safety evaluation of the food enzyme glucan 1,4‐α‐glucosidase from Trichoderma reesei (strain DP‐Nzh63)

EFSA Journal, 2019
The food enzyme 4‐α‐d‐glucan glucohydrolase (EC 3.2.1.3) is produced with a genetically modified Trichoderma reesei DP‐Nzh63 by Danisco US Inc. The genetic modifications do not give rise to safety concerns.
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

Stabilising normal and mis-sense variant alpha-glucosidase [PDF]

, 2006
alpha-Glucosidase (EC 3.2.1.3) is a lysosomal enzyme that hydrolyses alpha-1,4- and alpha-1,6-linkages of glycogen to produce free glucose. A deficiency in alpha-glucosidase activity results in glycogen storage disorder type II (GSD II), also called ...
Lang, Debbie, Revecca Kakavanos, Peter J. Meikle, Lang, D., Brooks, D., Hopwood, John J., Kakavanos, R., Kakavanos, Revecca, Meikle, Peter J., Hopwood, J., Meikle, P., John J. Hopwood, Debbie Lang, Doug A. Brooks, Brooks, Doug A.   +14 more
core   +1 more source

Safety of the food enzyme glucoamylase from a genetically modified Aspergillus niger (strain NZYM‐BF)

EFSA Journal, 2018
The food enzyme glucoamylase (glucan 1,4‐α‐glucosidase; EC 3.2.1.3) is produced with the genetically modified strain of Aspergillus niger by Novozymes A/S. The genetic modifications do not give rise to safety concerns. The food enzyme is free from viable
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, Klaus‐Dieter Jany, Sirpa Kärenlampi, André Penninks, Davor Želježic, Margarita Aguilera‐Gómez, Magdalena Andryszkiewicz, Davide Arcella, Ana Gomes, Natália Kovalkovičová, Yi Liu, Annamaria Rossi, Karl‐Heinz Engel, Andrew Chesson   +29 more
doaj   +1 more source

Structure and stability of glucoamylase II from Aspergillus niger: a circular dichroism study [PDF]

, 1984
Glucoamylase II (EC 3.2.1.3) from Aspergillus niger has 31 % α-helix, 36 % β-structure and rest aperiodic structure at pH 4.8 as analysed by the method of Provencher and Glockner (1981,Biochemistry, 20,33).
Appu Rao, A. G., Shenoy, B. C., Raghavendra Rao, M. R.   +2 more
core   +1 more source

Safety evaluation of the food enzyme glucan 1,4‐α‐glucosidase from a genetically modified Aspergillus niger (strain NZYM‐BW)

EFSA Journal, 2018
The food enzyme glucan 1,4‐α‐glucosidase (EC 3.2.1.3) is produced with the genetically modified Aspergillus niger strain NZYM‐BW by Novozymes A/S. The genetic modifications do not give rise to safety concerns. The food enzyme is free from viable cells of
EFSA Panel on Food Contact Materials, Enzymes and 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, Magdalena Andryszkiewicz, Ana Gomes, Natália Kovalkovičová, Yi Liu, Karl Heinz Engel, Andrew Chesson   +25 more
doaj   +1 more source

Hydrolysis of maize starch using amylolytic enzymes extracted from sorghum malt [PDF]

, 2010
Amylases, a-amylase (EC 3.2.1.1, α-1, 4-glucan-4-glucanohydrolase) and glucoamylase (EC 3.2.1.3, α-1, 4; α-1, 6-glucan glucohydrolase; amyloglucosidase), extracted and partially purified from sorghum maltwere used to hydrolyze maize starch.
A Adejumo, Layokun, S, Adejumo, A, F Agboola, Agboola, F, S Layokun   +5 more
core   +2 more sources