Results 31 to 40 of about 835 (125)
Digestive enzymes in Rhinolophus euryale (Rhinolophidae, Chiroptera) are active also during hibernation [PDF]
During the winter, bats use hibernation as a means of surviving the period of low prey offer. However, the Mediterranean horseshoe bat (Rhinolophus euryale) arouses from torpor quite frequently.
Maxinová, Edita +2 more
core +3 more sources
Interactional Effects of β-Glucan, Starch, and Protein in Heated Oat Slurries on Viscosity and In Vitro Bile Acid Binding [PDF]
Three major oat components, β-glucan, starch, and protein, and their interactions were evaluated for the impact on viscosity of heated oat slurries and in vitro bile acid binding. Oat flour from the experimental oat line “N979” (7.45% β-glucan) was mixed
Kim, Hyun Jung +2 more
core +3 more sources
Trends in breeding oat for nutritional grain quality - An overview [PDF]
Oat is an economically important crop and ranks sixth in world cereal production after maize, wheat, rice, barley and sorghum. It has been primarily utilized as livestock feed.
Abidi, I. +7 more
core +2 more sources
The food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase, EC 3.2.1.1) and 1,4‐α‐glucan 6‐α‐glucosyltransferase ((1→4)‐α‐d‐glucan:(1→4)‐α‐d‐glucan(d‐glucose) 6‐α‐d‐glucosyltransferase, EC 2.4.1.24) is produced with a Paenibacillus alginolyticus by ...
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP) +24 more
doaj +1 more source
Genetic diversity and genome wide association study of β-glucan content in tetraploid wheat grains [PDF]
Non-starch polysaccharides (NSPs) have many health benefits, including immunomodulatory activity, lowering serum cholesterol, a faecal bulking effect, enhanced absorption of certain minerals, prebiotic effects and the amelioration of type II diabetes ...
Blanco, Antonio +7 more
core +6 more sources
Safety evaluation of the food enzyme α‐amylase from Cellulosimicrobium funkei strain AE‐AMT
The food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the non‐genetically modified Cellulosimicrobium funkei strain AE‐AMT by Amano Enzyme Inc. The food enzyme is free from viable cells of the production organism.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP) +21 more
doaj +1 more source
Mass spectrometry-based proteomic analysis to characterise barley breeding lines [PDF]
Barley is a key ingredient in the malting and brewing industry, and it is the fourth most important crop being cultivated worldwide. The protein content of the barley grain is one of the main components determining the quality and nutritive value of the ...
Bahmani, Mahya
core +2 more sources
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) +28 more
doaj +1 more source
Safety evaluation of the food enzyme α-amylase from the genetically modified Bacillus licheniformis strain DP-Dzb52 [PDF]
[EN] The food enzyme alpha-amylase (1,4-alpha-D-glucan glucanohydrolase; EC 3.2.1.1) is produced with the genetically modified Bacillus licheniformis strain DP-Dzb52 by Danisco US Inc.
Alicja Mortensen +14 more
core +1 more source
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) +24 more
doaj +1 more source

