Agro-Morphological and Biochemical Characterization of Wild Prunus spinosa L. Subsp. dasyphylla (Schur) Domin Genotypes Naturally Grown in Western Black Sea Region of Turkey

In this study, agro-morphological, sensory and biochemical characteristics of 23 plum genotypes belonging to Prunus spinosa L. subsp. dasyphylla (Schur) Domin growing wild in the West Black Sea Region in Turkey were investigated. Agro-morphological, sensory and biochemical properties of genotypes were highly different from each other. Principal component analysis was performed to determine the correlation between these properties and genotypes. The variation in the study was determined to be 63.5% in agro-morphological properties, 53.8% in organic acids and 46% in phenolic compounds. In terms of fruit weight, 14BLM08 genotype (38.42 g) was determined to be superior to other genotypes. The fruit firmness value, which is important in the storage of fruits, was recorded as the highest in the 14BLM14 genotype (9.07 kg/cm2). Chlorogenic acid was higher than the other phenolic compounds and the highest value was obtained in the 14BLM20 (11.45 mg/kg) genotype. It was recorded that the value of malic acid, which is the major organic acid of the plums, varied between 269.65–1294.64 mg/100 g. Genotypes showed diverse vitamin C content, and the highest value was found in the 14BLM18 genotype as 54.42 mg/100g. Each genotype showed superiority according to the type of traits, and thus breeders may have used these genotypes as the superior ones for specific plum breeding purposes. In addition, these genotypes could be satisfactorily used in domestication.

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Biochemical characterization of specific Alanine Decarboxylase (AlaDC) and its ancestral enzyme Serine Decarboxylase (SDC) in tea plants (Camellia sinensis)

BMC Biotechnology ◽

10.1186/s12896-021-00674-x ◽

2021 ◽

Vol 21 (1) ◽

Author(s):

Peixian Bai ◽

Liyuan Wang ◽

Kang Wei ◽

Li Ruan ◽

Liyun Wu ◽

...

Keyword(s):

Gene Duplication ◽

Camellia Sinensis ◽

Biochemical Characterization ◽

Specific Activity ◽

Protein Sequences ◽

Biochemical Properties ◽

High Similarity ◽

New Gene ◽

Tea Plants

Abstract Background Alanine decarboxylase (AlaDC), specifically present in tea plants, is crucial for theanine biosynthesis. Serine decarboxylase (SDC), found in many plants, is a protein most closely related to AlaDC. To investigate whether the new gene AlaDC originate from gene SDC and to determine the biochemical properties of the two proteins from Camellia sinensis, the sequences of CsAlaDC and CsSDC were analyzed and the two proteins were over-expressed, purified, and characterized. Results The results showed that exon-intron structures of AlaDC and SDC were quite similar and the protein sequences, encoded by the two genes, shared a high similarity of 85.1%, revealing that new gene AlaDC originated from SDC by gene duplication. CsAlaDC and CsSDC catalyzed the decarboxylation of alanine and serine, respectively. CsAlaDC and CsSDC exhibited the optimal activities at 45 °C (pH 8.0) and 40 °C (pH 7.0), respectively. CsAlaDC was stable under 30 °C (pH 7.0) and CsSDC was stable under 40 °C (pH 6.0–8.0). The activities of the two enzymes were greatly enhanced by the presence of pyridoxal-5′-phosphate. The specific activity of CsSDC (30,488 IU/mg) was 8.8-fold higher than that of CsAlaDC (3467 IU/mg). Conclusions Comparing to CsAlaDC, its ancestral enzyme CsSDC exhibited a higher specific activity and a better thermal and pH stability, indicating that CsSDC acquired the optimized function after a longer evolutionary period. The biochemical properties of CsAlaDC might offer reference for theanine industrial production.

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Functional and Biochemical Characterization of Immunologically Derived Equine Platelet-Activating Factor

Veterinary Pathology ◽

10.1177/030098588502200413 ◽

1985 ◽

Vol 22 (4) ◽

pp. 375-386 ◽

Cited By ~ 6

Author(s):

H. C. Wimberly ◽

D. O. Slauson ◽

N. R. Neilsen

Keyword(s):

Functional Activity ◽

Biochemical Characterization ◽

Platelet Activating Factor ◽

Biochemical Properties ◽

Naturally Occurring ◽

Rabbit Platelets ◽

Rapid Reaction ◽

Specific Challenge

Antigen-specific challenge of equine leukocytes induced the non-lytic release of a platelet-activating factor in vitro. The equine platelet-activating factor stimulated the release of serotonin from equine platelets in a dose-responsive manner, independent of the presence of cyclo-oxygenase pathway inhibitors such as indomethacin. Rabbit platelets were also responsive to equine platelet-activating factor. The release of equine platelet-activating factor was a rapid reaction with near maximal secretion taking place in 30 seconds. Addition of equine platelet-activating factor to washed equine platelets stimulated platelet aggregation which could not be inhibited by the presence of aspirin or indomethacin. Platelets preincubated with equine platelet-activating factor became specifically desensitized to equine platelet-activating factor while remaining responsive to other platelet stimuli such as collagen and epinephrine. The following biochemical properties of equine platelet-activating factor are identical to those properties of 1-0-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine (AGEPC): stability upon exposure to air and acid; loss of functional activity after basecatalyzed methanolysis with subsequent acylation that returned all functional activity; and identical relative mobilities on silica gel G plates developed with chloroform:methanol:water (65:35:6, volume/volume). The combined functional and biochemical characteristics of equine platelet-activating factor strongly suggest identity between this naturally occurring, immunologically derived equine factor and AGEPC.

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Identification and Morphological-Physiological Characterization of Astaxanthin Producer Strains of Haematococcus pluvialis from the Black Sea Region

Applied Biochemistry and Microbiology ◽

10.1134/s0003683818060078 ◽

2018 ◽

Vol 54 (6) ◽

pp. 639-648

Author(s):

E. S. Chelebieva ◽

N. V. Dantsyuk ◽

K. A. Chekanov ◽

I. N. Chubchikova ◽

I. V. Drobetskaya ◽

...

Keyword(s):

Black Sea ◽

Haematococcus Pluvialis ◽

The Black Sea ◽

Black Sea Region ◽

Physiological Characterization ◽

Producer Strains

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Identification and biochemical characterization of a novel PP2C-like Ser/Thr phosphatase inE. coli

10.1101/303594 ◽

2018 ◽

Author(s):

Krithika Rajagopalan ◽

Jonathan Dworkin

Keyword(s):

Biochemical Characterization ◽

Regulatory Protein ◽

Biochemical Properties ◽

Bacterial Genomes ◽

Phosphatase Inhibitors ◽

E Coli ◽

Specificity And Sensitivity ◽

Genes Encoding ◽

Number Of Bacteria

AbstractIn bacteria, signaling phosphorylation is thought to occur primarily on His and Asp residues. However, phosphoproteomic surveys in phylogenetically diverse bacteria over the past decade have identified numerous proteins that are phosphorylated on Ser and/or Thr residues. Consistently, genes encoding Ser/Thr kinases are present in many bacterial genomes such asE. coli,which encodes at least three Ser/Thr kinases. Since Ser/Thr phosphorylation is a stable modification, a dedicated phosphatase is necessary to allow reversible regulation. Ser/Thr phosphatases belonging to several conserved families are found in bacteria. One family of particular interest are Ser/Thr phosphatases which have extensive sequence and structural homology to eukaryotic Ser/Thr PP2C phosphatases. These proteins, called eSTPs (eukaryotic-like Ser/Thr phosphatases), have been identified in a number of bacteria, but not inE. coli.Here, we describe a previously unknown eSTP encoded by anE. coliORF,yegK,and characterize its biochemical properties including its kinetics, substrate specificity and sensitivity to known phosphatase inhibitors. We investigate differences in the activity of this protein in closely relatedE. colistrains. Finally, we demonstrate that this eSTP acts to dephosphorylate a novel Ser/Thr kinase which is encoded in the same operon.ImportanceRegulatory protein phosphorylation is a conserved mechanism of signaling in all biological systems. Recent phosphoproteomic analyses of phylogenetically diverse bacteria including the model Gram-negative bacteriumE. colidemonstrate that many proteins are phosphorylated on serine or threonine residues. In contrast to phosphorylation on histidine or aspartate residues, phosphorylation of serine and threonine residues is stable and requires the action of a partner Ser/Thr phosphatase to remove the modification. Although a number of Ser/Thr kinases have been reported inE. coli, no partner Ser/Thrphosphatases have been identified. Here, we biochemically characterize a novel Ser/Thr phosphatase that acts to dephosphorylate a Ser/Thr kinase that is encoded in the same operon.

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Purification and biochemical characterization of a β-cyanoalanine synthase expressed in germinating seeds of Sorghum bicolor (L.) moench

Turkish Journal of Biochemistry ◽

10.1515/tjb-2017-0214 ◽

2018 ◽

Vol 43 (6) ◽

pp. 638-650

Author(s):

Ruth Ololade Amiola ◽

Adedeji Nelson Ademakinwa ◽

Zainab Adenike Ayinla ◽

Esther Nkechi Ezima ◽

Femi Kayode Agboola

Keyword(s):

Kinetic Parameters ◽

Biochemical Characterization ◽

Catalytic Properties ◽

Specific Activity ◽

Biochemical Properties ◽

Subunit Molecular Weight ◽

Cyanoalanine Synthase ◽

Germinating Seeds ◽

Sorghum Bicolor L

Abstract Background β-Cyanoalanine synthase plays essential roles in germinating seeds, such as in cyanide homeostasis. Methods β-Cyanoalanine synthase was isolated from sorghum seeds, purified using chromatographic techniques and its biochemical and catalytic properties were determined. Results The purified enzyme had a yield of 61.74% and specific activity of 577.50 nmol H2S/min/mg of protein. The apparent and subunit molecular weight for purified β-cyanoalanine synthase were 58.26±2.41 kDa and 63.4 kDa, respectively. The kinetic parameters with sodium cyanide as substrate were 0.67±0.08 mM, 17.60±0.50 nmol H2S/mL/min, 2.97×10−1 s−1 and 4.43×102 M−1 s−1 for KM, Vmax, kcat and kcat/KM, respectively. With L-cysteine as substrate, the kinetic parameters were 2.64±0.37 mM, 63.41±4.04 nmol H2S/mL/min, 10.71×10−1 s−1 and 4.06×102 M−1 s−1 for KM, Vmax, kcat and kcat/KM, respectively. The optimum temperature and pH for activity were 35°C and 8.5, respectively. The enzyme retained more than half of its activity at 40°C. Inhibitors such as HgCl2, EDTA, glycine and iodoacetamide reduced enzyme activity. Conclusion The biochemical properties of β-cyanoalanine synthase in germinating sorghum seeds highlights its roles in maintaining cyanide homeostasis.

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Biochemical Characterization of Traditional Varieties of Sweet Pepper (Capsicum annuum L.) of the Campania Region, Southern Italy

Antioxidants ◽

10.3390/antiox9060556 ◽

2020 ◽

Vol 9 (6) ◽

pp. 556 ◽

Cited By ~ 3

Author(s):

Florinda Fratianni ◽

Antonio d’Acierno ◽

Autilia Cozzolino ◽

Patrizia Spigno ◽

Riccardo Riccardi ◽

...

Keyword(s):

Ascorbic Acid ◽

Biochemical Characterization ◽

Principal Component ◽

Sweet Pepper ◽

Total Polyphenols ◽

Campania Region ◽

Polyphenol Profile ◽

Red Variety ◽

Β Carotene

Bioactive compounds of different Campania native sweet pepper varieties were evaluated. Polyphenols ranged between 1.37 mmol g−1 and 3.42 mmol g−1, β-carotene was abundant in the red variety “Cazzone” (7.05 μg g−1). Yellow and red varieties showed a content of ascorbic acid not inferior to 0.82 mg g−1, while in some green varieties the presence of ascorbic acid was almost inconsistent. Interrelationships between the parameters analyzed and the varieties showed that ascorbic acid could represent the factor mostly influencing the antioxidant activity. Polyphenol profile was different among the varieties, with a general prevalence of acidic phenols in yellow varieties and of flavonoids in red varieties. Principal Component Analysis, applied to ascorbic acid, total polyphenols and β-carotene, revealed that two of the green varieties (“Friariello napoletano” and “Friariello Sigaretta”) were well clustered and that the yellow variety “Corno di capra” showed similarity with the green varieties, in particular with “Friariello Nocerese”. This was confirmed by the interrelationships applied to polyphenol composition, which let us to light on a clustering of several red and yellow varieties, and that mainly the yellow ”Corno di capra” was closer to the green varieties of “Friariello”.

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