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From Low-Loaded Mesophilic to High-Loaded Thermophilic Anaerobic Digestion: Changes in Reactor Performance and Microbiome. [PDF]
Microb BiotechnolModin O +5 more
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A prescription for engineering PFAS biodegradation. [PDF]
Biochem JWackett LP, Robinson SL.
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Sustainable Production of Ulva Oligosaccharides via Enzymatic Hydrolysis: A Review on Ulvan Lyase. [PDF]
FoodsHuang A, Wu X, Lu F, Liu F.
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Integrated metabarcoding and culture-dependent assessments reveal <i>Pseudomonas</i> as dominant hyphosphere-pathobiont in Race 4 <i>Fusarium</i> wilt pathogen of cotton. [PDF]
Front MicrobiolAntony-Babu S +12 more
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Exploring the enzymatic repertoires of Bacteria and Archaea and their associations with metabolic maps. [PDF]
Braz J MicrobiolTenorio-Salgado S +4 more
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Plant Phenylalanine/Tyrosine Ammonia-lyases
Trends in Plant Science, 2020Aromatic amino acid deaminases are key enzymes mediating carbon flux from primary to secondary metabolism in plants. Recent studies have uncovered a tyrosine ammonia-lyase that contributes to the typical characteristics of grass cell walls and contributes to about 50% of the total lignin synthesized by the plant.
Jaime, Barros, Richard A, Dixon
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Phytochemistry, 1973
Abstract The literature concerning the physiology and biochemistry of the enzyme phenylalanine ammonia lyase (PAL) (E.C. 4.1.1.5) from different organisms has been reviewed. Levels of the enzyme are affected by age, light, phytochrome, wounding, infection and growth modifiers. The possibility that PAL is involved in the control of phenolic metabolism
Edith L. Camm, G.H.Neil Towers
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Abstract The literature concerning the physiology and biochemistry of the enzyme phenylalanine ammonia lyase (PAL) (E.C. 4.1.1.5) from different organisms has been reviewed. Levels of the enzyme are affected by age, light, phytochrome, wounding, infection and growth modifiers. The possibility that PAL is involved in the control of phenolic metabolism
Edith L. Camm, G.H.Neil Towers
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Artificial Cell-Microencapsulated Phenylalanine Ammonia-Lyase
Applied Biochemistry and Biotechnology, 1984Phenylalanine ammonia-lyase (PAL) is immobilized in collodion artificial cells. Once technical problems associated with the encapsulation of this enzyme were solved, the enzyme kinetics were compared to PAL in free solution. Microencapsulated PAL has an apparent enzyme activity that is 20% of the activity of enzyme in free solution.
L, Bourget, T M, Chang
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Phenylalanine ammonia-lyase entrapped in fibers
Biochimie, 1980Phenylalanine ammonia-lyase extracted form Rhodotorula rubra (IFO 1101) was immobilized into cellulose triacetate fibers made hemocompatible by physical blend with a platelet anti-aggregating agent. The entrapped enzyme could operate at physiological values of phenylalanine and tyrosine reducing their level to traces within a few hours.
W, Marconi +4 more
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