Results 31 to 40 of about 10,681 (161)

Safety evaluation of the food enzyme triacylglycerol lipase from the genetically modified Aspergillus niger strain NZYM‐DB

open access: yesEFSA Journal, 2021
The food enzyme triacylglycerol lipase (triacylglycerol acylhydrolase EC 3.1.1.3) is produced with a genetically modified Aspergillus niger strain NZYM‐DB by Novozymes A/S. The genetic modifications do not give rise to safety concerns. The food enzyme is
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +25 more
doaj   +1 more source

Early feeding to modify digestive enzyme activity in broiler chickens [PDF]

open access: yes, 2014
Objective. To evaluate the effect on digestive enzyme activity in broiler chickens by providing food in the first 48 hrs. after birth. Materials and methods.
Emma Rueda de A.   +3 more
core   +3 more sources

ISOLATION AND PURIFICATION OF LIPASE FROM COCOA BEANS (Theobroma cacao. L.) OF CLONE PBC 159

open access: yesIndonesian Journal of Chemistry, 2010
Lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) was extracted and purified from acetone dry powder of cocoa (Theobroma cacao. L.) of clone PBC 159 extract.
Ratna Agung Samsumaharto
doaj   +1 more source

Digestion of the mono- and diesters of hexane-1,6-diol by pancreatic lipase

open access: yesJournal of Lipid Research, 1972
The digestion in vitro by pancreatic lipase (EC 3.1.1.3) of the mono- and dioleate esters of hexane-1,6-diol has been studied. Under the conditions employed, the pathways for the lysis of these materials are proposed to be a hydrolysis step diester ...
F.H. Mattson, R.A. Volpenhein
doaj   +1 more source

Safety evaluation of the food enzyme triacylglycerol lipase from the non‐genetically modified Aspergillus luchuensis strain AE‐L

open access: yesEFSA Journal, 2023
The food enzyme triacylglycerol lipase (triacylglycerol acylhydrolase; EC 3.1.1.3) is produced with the non‐genetically modified Aspergillus luchuensis strain AE‐L 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)   +22 more
doaj   +1 more source

Green biosynthesis of rare DHA-phospholipids by lipase-catalyzed transesterification with edible algal oil in solvent-free system and catalytic mechanism study

open access: yesFrontiers in Bioengineering and Biotechnology, 2023
Docosahexaenoic acid (DHA)-enriched phosphatidylcholine (PC) has received significant scientific attention due to the health benefits in food and pharmaceutical products.
Tiantian Zhang   +7 more
doaj   +1 more source

Safety evaluation of the food enzyme triacylglycerol lipase from the genetically modified Trichoderma reseei strain AR‐822 [PDF]

open access: yesEFSA J
Abstract The food enzyme triacylglycerol lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) is produced with the genetically modified Trichoderma reseei strain AR‐822 by AB Enzymes GmbH. The genetic modifications do not give rise to safety concerns. The food enzyme is free from viable cells of the production organism and its DNA.
EFSA Panel on Food Enzymes (FEZ)   +17 more
europepmc   +2 more sources

Safety evaluation of the food enzyme triacylglycerol lipase from the genetically modified Aspergillus luchuensis strain FL105SC

open access: yesEFSA Journal, 2023
The food enzyme triacylglycerol lipase (triacylglycerol acylhydrolase; EC 3.1.1.3) is produced with the genetically modified Aspergillus luchuensis strain FL105SC by Advanced Enzyme Technologies Ltd.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +23 more
doaj   +1 more source

Structural basis of the chiral selectivity of Pseudomonas cepacia lipase [PDF]

open access: yes, 1998
To investigate the enantioselectivity of Pseudomonas cepacia lipase, inhibition studies were performed with SC- and RC-(RP,SP)-1,2-dialkylcarbamoylglycero-3-O-p-nitrophenyl alkylphosphonates of different alkyl chain lengths. P.
Dijkstra, Bauke W.,   +4 more
core   +2 more sources

Relative rates of hydrolysis by rat pancreatic lipase of esters of C2-C18 fatty acids with C1-C18 primary n-alcohols

open access: yesJournal of Lipid Research, 1969
The rate at which rat pancreatic lipase (glycerol-ester hydrolase, EC 3.1.1.3) hydrolyzes the esters of primary n-alcohols containing from 1 to 18 carbon atoms with fatty acids containing from 2 to 18 carbon atoms was determined.
F.H. Mattson, R.A. Volpenhein
doaj   +1 more source

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