Results 71 to 80 of about 6,120 (217)
An Update: Enzymatic Synthesis for Industrial Applications
Angewandte Chemie International Edition, Volume 64, Issue 27, July 1, 2025.Biocatalysis has become a sustainable and cost‐competitive alternative to established chemical synthesis, enabling the enzyme‐based production of not only commodity chemicals but (non‐natural) amino acids, (rare) sugars, as well as synthetic nucleotides.
Thomas Bayer +4 more
wiley +1 more source
Molecular aspects and comparative genomics of bacteriophage endolysins [PDF]
, 2013 Phages are recognized as the most abundant and diverse entities on the planet. Their diversity is predominantly determined by their dynamic adaptation capacities, when confronted with different selective pressures in an endless cycle of co-evolution with
Azeredo, Joana +7 more
core +1 more source
Crop Science, Volume 65, Issue 4, July/August 2025.Abstract The consumption of plant proteins is increasing worldwide as a viable alternative to animal‐derived proteins in the marketplace. The projected increase in global population to at least 10 billion by 2050 is placing greater pressure on the food supply, particularly due to the rising demand for large‐scale protein production.
H. A. Cordoba +22 more
wiley +1 more source
Properties of rat liver N-acylethanolamine amidohydrolase.
Journal of Biological Chemistry, 1985 Rat liver microsomes and mitochondria contain an amidohydrolase which catalyzes the hydrolysis of N-acylethanolamine to ethanolamine and fatty acid. The enzyme is active over a wide range of pH, does not require divalent cations, and is inhibited by sulfhydryl-reactive agents.
M. L. Zuzarte-Augustin +2 more
openaire +3 more sources
Biochemical properties of penicillin amidohydrolase from Micrococcus luteus [PDF]
Applied and Environmental Microbiology, 1979 Some biochemical properties of whole-cell penicillin amidohydrolase from Micrococcus luteus have been studied. This whole-cell enzyme showed its maximal activity at 36 degrees C at pH 7.5. It was found that the activation energy of this enzyme was 8.03 kcal (ca. 33.6 kJ) per mol, and this amidohydrolase showed first-order decay at 36 degrees C.
Dewey D. Y. Ryu, D. H. Nam
openaire +2 more sources
Функционирование некоторых амидогидролаз в черноземе, загрязненном соединениями фтора [PDF]
, 2009 Дослiджено функцiонування амiдогiдролаз (аспарагiнази, глутамiнази, уреази i аргiнази), а також дезамiназ (амiдази) в чорноземах, забруднених сполуками фтору.
Гришко, В.Н.
core
Enzyme activities in soils as affected by management practices [PDF]
, 2002 Studies were undertaken to investigate the long-term effects of lime application and tillage systems (no-till, ridge-till, and chisel plow) on soil microbial biomass C (Cmic) and N (Nmic) and the activities of glycosidases (alpha- and beta-glucosidases ...
Ekenler, Mine
core +3 more sources
Combined Forces Against Bacteria: Phages and Antibiotics
Health Science Reports, Volume 8, Issue 7, July 2025.ABSTRACT Background and Aim It is now known that bacteria are highly interactive and exhibit a range of complex cooperative behaviors, including conjugal plasmid transfer, toxins, swarming, drug resistance, toxin production, biofilm development, and other virulence traits.
Shima Afrasiabi +3 more
wiley +1 more source
Anandamide Amidohydrolase Activity in Rat Brain Microsomes [PDF]
Journal of Biological Chemistry, 1995 An amidohydrolase activity present in rat brain microsomes catalyzes the hydrolysis of N-arachidonoyl-[3H]ethanolamine ([3H]anandamide), an endogenous cannabimimetic substance, forming [3H]ethanolamine and arachidonic acid. Amidohydrolase activity is maximal at pH 6 and 8, is independent of divalent cations, has an apparent Km for [3H]anandamide of 12 ...
Desarnaud, Franck +2 more
openaire +5 more sources
EFSA Journal, Volume 23, Issue 7, July 2025.Abstract The asparaginase (L‐asparagine amidohydrolase, EC 3.5.1.1) is produced by the non‐genetically modified Saccharomyces cerevisiae strain ARY‐2 by Renaissance BioScience Corporation. The food enzyme is not separated from the yeast cells during the enzyme production. The food enzyme is intended to be used to reduce acrylamide formation during food
EFSA Panel on Food Enzymes (FEZ) +16 more
wiley +1 more source