Search

Capsicum is one of the most important and diverse plant taxa, widely used as a spice and vegetable worldwide, including Turkey. Germplasm characterization is an essential step for crop breeding. In the present study, we characterized the genetic diversity and population structure of a collection of 94 pepper accessions using inter-primer binding site (iPBS) retrotransposon-based markers. A total of 20 iPBS primers were used that generated 172 bands (mean = 8.6 bands/primer), of which ~92% were polymorphic in the entire germplasm collection, whereas 83%, 69%, and 80% of the bands were polymorphic within the C. annuum, C. chinense, and C. frutescens subsets, respectively. All of the taxa analyzed were clearly differentiated by the iPBS markers. The polymorphism information content of the markers ranged between 0.15 and 0.99, with an average of 0.66. Cluster analyses by different methods (UPGMA, STRUCTURE, and principal coordinate analysis) revealed a clear separation of all of the C. annuum accessions from the other pepper species, with a few subclusters observed among the latter, including groups with accessions of both C. frutescens and C. chinense. At the interspecies level, the 3 clustering methods clearly discriminated C. annuum from C. frutescens and C. chinense. No clear association was found between the iPBS-based clustering and geographical origin or fruit characteristics of the accessions. This is the first report characterizing the genetic diversity and population structure in the Turkish pepper germplasm using iPBS markers. It is expected that these data will serve as a foundation for the development of new and improved pepper varieties. [ABSTRACT FROM AUTHOR]

Laurel is a medicinally important plant and is known to the world for its essential oil. Turkey is the main market in the laurel leaf trade by sharing about 90% of the world trade. Here we made an effort to elucidate genetic diversity and population structure of 94 Turkish laurel genotypes collected from 26 provinces and four geographical regions using inter-primer binding site (iPBS) retrotransposon markers. A total of 13 most polymorphic primers were selected which yielded 195 total bands, of which 84.10% were found polymorphic. Mean polymorphism information content (PIC) was (0.361) and diversity indices including mean effective number of alleles (1.36), mean Shannon's information index (0.35) and overall gene diversity (0.22) revealed the existence of sufficient amount of genetic diversity in the studied plant material. Most diversity was found in genotypes collected from the Mediterranean region. Analysis of molecular variance (AMOVA) revealed that most of the variation (85%) in Turkish laurel germplasm is due to differences within populations. Model-based structure, principal coordinate analysis (PCoA) and neighbor-joining algorithms were found in agreement and clustered the studied germplasm according to their collection provinces and regions. This is a very first study exploring the genetic diversity and population structure of laurel germplasm using iPBS-retrotransposon marker system. We believe that information provided in this work will be helpful for the scientific community to take more interest in this forgotten but the medicinally important plant. [ABSTRACT FROM AUTHOR]

Background: γ-glucosidase (EC 3.2.1.21) catalyzing the γ-glycosidic linkages in polysaccharides is a ubiquitous enzyme with great importance in biofuel and other industries. Enzyme inhibition by glucose has been considered as the major hurdle in the practical applications of this enzyme. Therefore, there has been a continuous search for novel γ-glucosidase with high glucose tolerance and stability at industrial temperature. In the present study, recombinant of γ-glucosidase from Thermococcus radiotolerans has been produced and characterized. Results: The enzyme was overexpressed in Escherichia coli strain BL21 (DE3) codon plus RIPL and purified by selective heat denaturation, ethanol precipitation and anion exchange chromatography. Purified enzyme displayed a band on SDS-PAGE with a molecular weight of 50 kDa. Optimum enzyme activity was found at pH 5, and 85°C, it retained more than 46% activity when incubated at 100°C for 5 min and exhibited 80% activity in the presence of 800 mM glucose. Km and Vmax values of the purified enzyme were found as 16.3 mM of pNPG and 25.8 μ moles per min. Molecular docking studies have shown a strong binding affinity of pNPG with the enzyme active site consisting of Glu365, Asn266, and Trp295 as major the active site amino acids. MD simulation analysis has shown a significantly high stability of enzyme active site and high potential of enzyme substrate complex formation. [ABSTRACT FROM AUTHOR]