Amalia Afendra

Amalia Afendra
University of Ioannina | UOI · Department of Biological Applications and Technologies

PhD

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24
Publications
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487
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Publications

Publications (24)
Article
Full-text available
Background: Microbial lipases catalyze a broad spectrum of reactions and are enzymes of considerable biotechnological interest. The focus of this study was the isolation of new lipase genes, intending to discover novel lipases whose products bear interesting biochemical and structural features and may have a potential to act as valuable biocatalys...
Article
Full-text available
We have recently (8th February 2018) published our article entitled “Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) from Stenotrophomonas maltophilia Psi-1, the first member of a new bacterial lipase family (XVIII)” [1]. While our manuscript was going through the final stages of publication, an article by Samoyl...
Article
Full-text available
The kinetics of immobilized enzymes can not be analyzed by means of the simple Michaelis-Menten concept, which generally fails to describe the immobilized state due to both its probable barriers, and because the active concentration of the enzyme approaches, or even exceeds this of its substrate(s). In such cases, the various experimental data are...
Article
Full-text available
Comparative in silico analyses of bacterial RNase P enzymes clustered their RNA subunits in type A RNA, found in E. coli, and in type B, found in B. subtilis. Zymomonas mobilis RNase P consists of one protein (Zmo-RnpA) and one type A RNA (RPR) subunit containing the P19 element, present in many RNase P RNAs of any structure class, but is lacking i...
Article
This is a short recollection of C. Drainas research and memoirs on occasion of his untimely death.
Article
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A hyperthermophilic alpha-amylase encoding gene from Pyrococcus woesei was transferred and expressed in Xanthomonas campestris ATCC 13951. The heterologous alpha-amylase activity was detected in the intracellular fraction of X. campestris and presented similar thermostability and catalytic properties with the native P. woesei enzyme. The recombinan...
Article
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Moderately halophilic bacteria (MHB) of the genera Halomonas and Chromohalobacter have been used as hosts for the expression of heterologous proteins of biotechnological interest, thus expanding their potential to be used as cell factories for various applications. This chapter deals with the methodology for the construction of recombinant plasmids...
Article
MbeA is a 60 kDa protein encoded by plasmid ColE1. It plays a key role in conjugative mobilization. MbeA*, a slightly truncated version of MbeA, was purified for in vitro analysis. MbeA* catalysed DNA cleavage and strand-transfer reactions using oligonucleotides embracing the ColE1 nic site, which was mapped to 5'-(1469)CTGG/CTTA(1462)-3'. Thus Mbe...
Article
Two recombinant plasmids, expressing ice nucleation activity, were constructed and named pCPP30inaZ and pCPP38inaZ. They were transferred to the ice-negative, xanthan-producing Xanthomonas campestris pv. campestris by electroporation. The transformants were used for co-production of xanthan gum and ice nuclei from sugar beet molasses. The highest v...
Article
We investigated the applicability of the green fluorescent protein of Aequorea victoria as a reporter for gene expression in the strictly fermentative Gram-negative ethanologenic bacterium Zymomonas mobilis and in the moderately halophilic bacterium Halomonas elongata. We have succeeded to express a mutated gene of green fluorescent protein under t...
Article
The complete nucleotide sequences of two small cryptic Zymomonas mobilis ATCC 10988 plasmids (pZMO1 and pZMO2) were determined. The plasmids showed 67% homology to each other at their nucleotide level. Plasmid pZMO1 was 1651 bp long with 38% G + C content and contained an open reading frame (ORFZMO1) of 1044 nucleotides. ORFZMO1 is predicted to enc...
Article
The 2.7-kb Zymomonas mobilis ATCC10988 plasmid pZMO3 contains a coding region (ORF1) indispensable for mobilization. A cis-acting 409-bp sequence between ORF2 (C-terminal) and ORF1 (N-terminal) conferred mobilization activity to pUC19, when the product of ORF1 was provided in trans. In this area, two segments showed homology with previously charact...
Article
Full-text available
A new recombinant plasmid, pBZIP1, was constructed for heterologous expression of high levels of ice nucleation activity in ethanol-producing Zymomonas mobilis strains CP4 and NCIB 11163. The plasmid construct contained the mobilization region and tetracycline resistance gene of pBR325, the replication region of the Z. mobilis native plasmid pZMO3...
Article
Full-text available
The advent of molecular genetics not only made possible analysis of disease mechanisms at a level of resolution not previously possible, but also provided the necessary tools to genetically engineer into plants new capabilities for self-defence against pathogens. In the case of bacterial pathogens, the study of genes and mechanisms of pathogenesis...
Article
Zymomonas mobilis plasmid pZMO3, equivalent to pZM2 the complete nucleotide sequence of which has been published (Misawa and Nakamura, 1989), expressed mobilisation functions in Escherichia coli JM83 and RR1 when fused to the HindIII site of pUC19. Experimental evidence based on filter mating and DNA sequence analysis supports that an ORF of pZMO3...
Article
A recombinant plasmid was constructed by ligating EcoRI digests of the plasmid cloning vector pBR325 and pZMO2, one of the natural plasmids of Zymomonas mobilis ATCC 10988. This vector, named pDS212 (total size 7.9 kb), which was able to transform Escherichia coli efficiently, was also transferred to Z. mobilis hosts by mobilization during conjugat...

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