Results 21 to 30 of about 2,061 (130)

Safety evaluation of the food enzyme α‐amylase from the non‐genetically modified Aspergillus sp. strain FUA [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 Aspergillus sp. strain FUA by DSM Food Specialties B.V. The food enzyme is free from viable cells of the production organism.
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, Cristina Fernàndez‐Fraguas, Magdalena Andryszkiewicz, Natalia Kovalkovicova, Eleonora Marini, Yi Liu   +18 more
doaj   +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

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

Analysis of Microbial Community Structure and Functional Genes for Volatile Flavor in Stinky Tofu. [PDF]

Food Sci Nutr
This study integrated metagenomics to decipher the core microbiota (e.g., Pseudomonas, Acinetobacter, Enterobacter) and functional genes governing volatile flavor biosynthesis in stinky tofu. Key enzymes like glycoside hydrolases and alcohol dehydrogenases catalyzed carbohydrate and amino acid metabolism, generating characteristic compounds such as ...
Luo A, Liu L, Shi S, Liu X, Hu B.
europepmc   +2 more sources

Safety evaluation of the food enzyme α‐amylase from the non‐genetically modified Bacillus amyloliquefaciens strain BA

EFSA Journal, 2023
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 BA by HBI Enzymes Inc.
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, Yrjö Roos, Magdalena Andryszkiewicz, Kyriaki Apergi, Cristina Fernàndez‐Fraguas, Yi Liu, Silvia Peluso, Giulio diPiazza, Andrew Chesson   +24 more
doaj   +1 more source

Importance of Inactivation Methodology in Enzymatic Processing of Raw Potato Starch: NaOCl as Efficient α-Amylase Inactivation Agent

Molecules, 2023
Efficient inactivation of microbial α-amylases (EC 3.2.1.1) can be a challenge in starch systems as the presence of starch has been shown to enhance the stability of the enzymes.
Signe Schram Zinck, Stefan Jarl Christensen, Ole Bandsholm Sørensen, Birte Svensson, Anne S. Meyer   +4 more
doaj   +1 more source

The response to selection in Glycoside Hydrolase Family 13 structures: A comparative quantitative genetics approach. [PDF]

PLoS ONE, 2018
The Glycoside Hydrolase Family 13 (GH13) is both evolutionarily diverse and relevant to many industrial applications. Its members hydrolyze starch into smaller carbohydrates and members of the family have been bioengineered to improve catalytic function ...
Jose Sergio Hleap, Christian Blouin
doaj   +1 more source

Atividade de enzimas relacionadas com a mobilização de carboidratos durante a dormência da nogueira (Juglans Regia) Walnut enzyme activity related with carbohydrate mobilization during dormancy period

Revista Brasileira de Fruticultura, 2009
A brotação da nogueira é dependente da mobilização de carboidratos do lenho para as gemas localizadas na porção superior dos ramos. O objetivo do trabalho foi contribuir para o entendimento do mecanismo de brotação acrótona da nogueira, em clima ...
Idemir Citadin, Agnès Guilliot, Marc Bonhomme, Rémy Rageau   +3 more
doaj   +1 more source

بهینه‌سازی تولید آنزیم آمیلاز در باکتری مقاوم به سرمای sp. ATR812 Janthinobacterium با استفاده از روشResponse Surface Methodology [PDF]

زیست‌شناسی کاربردی, 2018
آمیلاز (EC 3.2.1.1) یکی از مهم‌ترین آنزیم های صنعتی است که کاربردهای گسترده‌ای در صنایع مختلف دارد. این آنزیم پیوند گلیکوزیدی (4-1) α را در نشاسته هیدرولیز کرده و محصولاتی با وزن مولکولی کمتر مثل گلوکز، مالتوز و مالتوتریوز تولید می‌کند.
راضیه قاضی بیرجندی, بهار شهنواز, معصومه بحرینی, مریم محجوبین تهران   +3 more
doaj   +1 more source