scholarly journals Evaluation of physicochemical properties and enzymatic activity of organic substrates during four crop cycles in soilless containers

2018 ◽  
Vol 6 (8) ◽  
pp. 2066-2078 ◽  
Author(s):  
Pedro A. Mejia Guerra ◽  
Maria del Carmen Salas Sanjúan ◽  
Maria J. López
Keyword(s):  
Enzymatic Activity ◽  
Physicochemical Properties ◽  
Organic Substrates

The role of an urban park's tree stand in shaping the enzymatic activity, glomalin content and physicochemical properties of soil

2020 ◽  
Vol 741 ◽  
pp. 140446 ◽  
Author(s):  
Joanna Lemanowicz ◽  
Samir A. Haddad ◽  
Agata Bartkowiak ◽  
Robert Lamparski ◽  
Piotr Wojewódzki
Keyword(s):  
Enzymatic Activity ◽  
Physicochemical Properties ◽  
Tree Stand ◽  
Properties Of Soil

scholarly journals Ternary glycerol-based deep eutectic solvents: Physicochemical properties and enzymatic activity

2021 ◽  
Author(s):  
Shahidah Nusailah Rashid ◽  
Adeeb Hayyan ◽  
Maan Hayyan ◽  
Mohd Ali Hashim ◽  
Amal A.M Elgharbawy ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Physicochemical Properties ◽  
Deep Eutectic Solvents

scholarly journals AFM study of changes in properties of horseradish peroxidase after incubation of its solution near a pyramidal structure

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Yuri D. Ivanov ◽  
Tatyana O. Pleshakova ◽  
Ivan D. Shumov ◽  
Andrey F. Kozlov ◽  
Irina A. Ivanova ◽  
...  
Keyword(s):  
Horseradish Peroxidase ◽  
Enzymatic Activity ◽  
Physicochemical Properties ◽  
Noise Suppression ◽  
Protein Secondary Structure ◽  
Attenuated Total Reflection ◽  
Buffer Solution ◽  
Pyramidal Structure ◽  
Structure Changes ◽  
Anechoic Chambers

AbstractIn our present paper, the influence of a pyramidal structure on physicochemical properties of a protein in buffer solution has been studied. The pyramidal structure employed herein was similar to those produced industrially for anechoic chambers. Pyramidal structures are also used as elements of biosensors. Herein, horseradish peroxidase (HRP) enzyme was used as a model protein. HRP macromolecules were adsorbed from their solution onto an atomically smooth mica substrate, and then visualized by atomic force microscopy (AFM). In parallel, the enzymatic activity of HRP was estimated by conventional spectrophotometry. Additionally, attenuated total reflection Fourier-transform infrared spectroscopy (ATR-FTIR) has been employed in order to find out whether or not the protein secondary structure changes after the incubation of its solution either near the apex of a pyramid or in the center of its base. Using AFM, we have demonstrated that the incubation of the protein solution either in the vicinity of the pyramid’s apex or in the center of its base influences the physicochemical properties of the protein macromolecules. Namely, the incubation of the HRP solution in the vicinity of the top of the pyramidal structure has been shown to lead to an increase in the efficiency of the HRP adsorption onto mica. Moreover, after the incubation of the HRP solution either near the top of the pyramid or in the center of its base, the HRP macromolecules adsorb onto the mica surface predominantly in monomeric form. At that, the enzymatic activity of HRP does not change. The results of our present study are useful to be taken into account in the development of novel biosensor devices (including those for the diagnosis of cancer in humans), in which pyramidal structures are employed as sensor, noise suppression or construction elements.

The folding capacity of the mature domain of the dual-targeted plant tRNA nucleotidyltransferase influences organelle selection

2013 ◽  
Vol 453 (3) ◽  
pp. 401-412 ◽  
Author(s):  
Matthew Leibovitch ◽  
Daniela Bublak ◽  
Pamela J. Hanic-Joyce ◽  
Bodo Tillmann ◽  
Nadine Flinner ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Physicochemical Properties ◽  
Single Gene ◽  
Transit Peptide ◽  
Intracellular Distribution ◽  
Peptide Sequence ◽  
Mature Protein ◽  
Nuclear Targeting ◽  
Mature Domain ◽  
Cellular Compartments

tRNA-NTs (tRNA nucleotidyltransferases) are required for the maturation or repair of tRNAs by ensuring that they have an intact cytidine-cytidine-adenosine sequence at their 3′-termini. Therefore this enzymatic activity is found in all cellular compartments, namely the nucleus, cytoplasm, plastids and mitochondria, in which tRNA synthesis or translation occurs. A single gene codes for tRNA-NT in plants, suggesting a complex targeting mechanism. Consistent with this, distinct signals have been proposed for plastidic, mitochondrial and nuclear targeting. Our previous research has shown that in addition to N-terminal targeting information, the mature domain of the protein itself modifies targeting to mitochondria and plastids. This suggests the existence of an as yet unknown determinate for the distribution of dual-targeted proteins between these two organelles. In the present study, we explore the enzymatic and physicochemical properties of tRNA-NT variants to correlate the properties of the enzyme with the intracellular distribution of the protein. We show that alteration of tRNA-NT stability influences its intracellular distribution due to variations in organelle import capacities. Hence the fate of the protein is determined not only by the transit peptide sequence, but also by the physicochemical properties of the mature protein.

scholarly journals Effect of heteroatoms on the optical properties and enzymatic activity of N-doped carbon dots

RSC Advances ◽  
2021 ◽  
Vol 11 (31) ◽  
pp. 18776-18782
Author(s):  
Ahyun Lee ◽  
Sohee Yun ◽  
Eun Soo Kang ◽  
Jung Wan Kim ◽  
Jeong Ho Park ◽  
...  
Keyword(s):  
Optical Properties ◽  
Enzymatic Activity ◽  
Physicochemical Properties ◽  
Chemical Bonding ◽  
Carbon Dots ◽  
Dopant Content ◽  
Optical Applications ◽  
Doped Carbon Dots ◽  
The Relationship

The characteristics of N-CDs suitable for their optical applications or for use as nanozymes were demonstrated by rationalizing the relationship between the dopant content (e.g., the amount of doped N and types of chemical bonding) and physicochemical properties.

scholarly journals Physicochemical properties and enzymatic activity of wheat germ extract microencapsulated with spray and freeze drying

2021 ◽  
Vol 9 (2) ◽  
pp. 1192-1201
Author(s):  
Fahimeh Jamdar ◽  
Seyed Ali Mortazavi ◽  
Mohammad Reza Saiedi Asl ◽  
Akram Sharifi
Keyword(s):  
Enzymatic Activity ◽  
Physicochemical Properties ◽  
Wheat Germ ◽  
Freeze Drying ◽  
Wheat Germ Extract
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