Results 11 to 20 of about 740,354 (168)

Human salivary α‐amylase (EC.3.2.1.1) activity and periodic acid and schiff reactive (PAS) staining: A useful tool to study polysaccharides at an undergraduate level [PDF]

Biochemistry and Molecular Biology Education, 2006
AbstractHealth science education is presently in discussion throughout Europe due to the Bologna Declaration. Teaching basic sciences such as biochemistry in a health sciences context, namely in allied heath education, can be a challenging task since the students of preclinical health sciences are not often convinced that basic sciences are clinically ...
Fernandes, Ruben, Correia, Rossana, Fonte, Rosália, Prudêncio, Cristina   +3 more
openaire   +5 more sources

Safety evaluation of an extension of use of the food enzyme α‐amylase from the non‐genetically modified Bacillus amyloliquefaciens strain AE‐BAA [PDF]

EFSA Journal
The food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the non‐genetically modified microorganism Bacillus amyloliquefaciens strain AE‐BAA by Amano Enzyme Inc.
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, Monika Sramkova, Henk Van Loveren, Laurence Vernis, Daniele Cavanna, Giulio diPiazza, Yi Liu   +16 more
doaj   +2 more sources

Safety evaluation of the food enzyme α‐amylase from the genetically modified Bacillus licheniformis strain DP‐Dzb106 [PDF]

EFSA Journal
The food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the genetically modified Bacillus licheniformis strain DP‐Dzb106 by Genencor International B.V.
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 Solano, Henk Van Loveren, Laurence Vernis, Silvia Peluso, Magdalena Andryszkiewicz, Daniele Cavanna, Yi Liu   +16 more
doaj   +2 more sources

EC 3.2.1.1 [PDF]

, 2019
openaire   +2 more sources

Safety evaluation of the food enzyme containing trypsin, chymotrypsin, α‐amylase and triacylglycerol lipase from porcine pancreas

EFSA Journal, 2022
The food enzyme complex, containing trypsin (EC 3.4.21.4), chymotrypsin (EC 3.4.21.1), α‐amylase (1,4‐α‐d‐glucan glucanohydrolase, EC 3.2.1.1) and triacylglycerol lipase (triacylglycerol acylhydrolase, EC 3.1.1.3), is obtained from porcine pancreas by ...
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, Ursula Gundert‐Remy, Lieve Herman, Dominique Turck, Magdalena Andryszkiewicz, Natália Kovalkovičová, Joaquim Maia, Yi Liu, Rainieri Sandra, Andrew Chesson   +26 more
doaj   +1 more source

Safety evaluation of a food enzyme with glucan 1,4‐α‐glucosidase and α‐amylase activities from the genetically modified Aspergillus niger strain NZYM‐BX

EFSA Journal, 2021
The food enzyme with glucan 1,4‐α‐glucosidase (EC 3.2.1.3) and α‐amylase (EC 3.2.1.1) activities is produced with the genetically modified strain of Aspergillus niger NZYM‐BX by Novozymes A/S. The genetic modifications do not give rise to safety concerns.
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, Lieve Herman, Jaime Aguilera, Magdalena Andryszkiewicz, Natalia Kovalkovikova, Yi Liu, Andrew Chesson   +23 more
doaj   +1 more source

Utilization of α-amylase (EC 3.2.1.1) resistant maize and pea (Pisum sativum) starch in the rat [PDF]

British Journal of Nutrition, 1989
1. The extent of utilization of α-amylase (EC 3.2.1.1)-resistant retrograded starches in vivo was assessed in male Wistar rats (about 100 g body-weight). All animals were given a fibre-free semi-synthetic basal diet (SS) containing sucrose as the only carbohydrate source, ad lib., for 13 d. On day 14, after an overnight fast, rats were allocated to one
R M, Faulks, S, Southon, G, Livesey
openaire   +2 more sources

The level and origin of amylase (EC 3.2.1.1) in the digestive tract of chicks receiving trypsin inhibitors in their diet [PDF]

British Journal of Nutrition, 1978
1. Amylase (EC 3.2.1.1) activity found in the intestinal tract of chicks posterior to the stomach is of endogenous origin, as amylase in the food is inactivated by the low pH in the stomachs.2. Ingestion of raw soya-bean diet (RSD) or of heated soya-bean diet (HSD) supplemented with trypsin inhibitors induced higher amylase activities in the lower part
Z, Nitsan, Z, Madar
openaire   +2 more sources

α-Amylase (EC 3.2.1.1) susceptibility rather than viscosity or gastric emptying rate controls plasma responses to starch in healthy humans [PDF]

British Journal of Nutrition, 1990
The relationship between starch α-amylase (EC3.2.1.1) susceptibility, plasma responses and gastric emptying rates has been investigated in humans. Nine randomly chosen healthy subjects were given three carbohydrate test meals (25 g starch or equivalent glucose units): two maize starch pastes with (a) 240 (S24) or (b) 500 (S50) g amylose/kg, and a ...
F R, Bornet, Y, Bizais, S, Bruley des Varannes, B, Pouliquen, J, Delort Laval, J P, Galmiche   +5 more
openaire   +2 more sources

Statistical Based Bioprocess Design for Improved Production of Amylase from Halophilic Bacillus sp. H7 Isolated from Marine Water

Molecules, 2021
Amylase (EC 3.2.1.1) enzyme has gained tremendous demand in various industries, including wastewater treatment, bioremediation and nano-biotechnology. This compels the availability of enzyme in greater yields that can be achieved by employing potential ...
J. N. Bandal, V. A. Tile, R. Z. Sayyed, H. P. Jadhav, N. I. Wan Azelee, Subhan Danish, Rahul Datta   +6 more
doaj   +1 more source