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1.
Plant Dis ; 108(6): 1491-1500, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38780477

ABSTRACT

Ceratocystis manginecans has caused significant losses in forestry productivity in Indonesia and neighboring nations. It also infects horticultural trees, but the host range of individual isolates of C. manginecans is poorly studied. So, this study aimed to better understand the potential host range and evaluate aggressiveness against forestry and fruit tree species of C. manginecans isolated from various tree species in Indonesia. Five C. manginecans isolates, four from different tree species and one from the shot-hole borer Euwallacea perbrevis, were used to inoculate seven fruit and six forest tree species, including E. pellita and Acacia mangium. Many of the inoculated trees produced typical canker disease symptoms, such as rough, swollen, and cracked lesions on the bark, but some trees did not have any external symptoms. Mortality in the most susceptible clone of A. mangium was 40% within 8 weeks. Forest tree species were more susceptible than fruit trees, with the length of xylem discoloration ranging from 0.4 to 101 cm. In fruit trees, the average extent of xylem discoloration was lower, ranging from 0.4 to 20.5 cm; however, mortalities were recorded in two fruit tree species, Citrus microcarpa and Durio zibethinus. Host-isolate interaction was evident; isolate Ep106C from Eucalyptus pellita caused the greatest xylem discoloration in Citrus sp., whereas Hy163C from Hymenaea courbaril was the most damaging in D. zibethinus, Artocarpus heterophyllus, and Mangifera indica. Increasingly globalized food and fiber systems increase risk of disease spread, and the serious threat of C. manginecans incursions into countries where it is not present must be evaluated more thoroughly.


Subject(s)
Forestry , Plant Diseases , Trees , Plant Diseases/microbiology , Plant Diseases/parasitology , Ascomycota/physiology , Ascomycota/isolation & purification , Host Specificity , Indonesia , Animals , Fruit/microbiology , Acacia/microbiology
2.
ACS Appl Mater Interfaces ; 5(19): 9752-9, 2013 Oct 09.
Article in English | MEDLINE | ID: mdl-24028609

ABSTRACT

Efficient nanotextured black silicon solar cells passivated by an Al2O3 layer are demonstrated. The broadband antireflection of the nanotextured black silicon solar cells was provided by fabricating vertically aligned silicon nanowire (SiNW) arrays on the n(+) emitter. A highly conformal Al2O3 layer was deposited upon the SiNW arrays by the thermal atomic layer deposition (ALD) based on the multiple pulses scheme. The nanotextured black silicon wafer covered with the Al2O3 layer exhibited a low total reflectance of ∼1.5% in a broad spectrum from 400 to 800 nm. The Al2O3 passivation layer also contributes to the suppressed surface recombination, which was explored in terms of the chemical and field-effect passivation effects. An 8% increment of short-circuit current density and 10.3% enhancement of efficiency were achieved due to the ALD Al2O3 surface passivation and forming gas annealing. A high efficiency up to 18.2% was realized in the ALD Al2O3-passivated nanotextured black silicon solar cells.

3.
Mol Biotechnol ; 23(1): 1-10, 2003 Jan.
Article in English | MEDLINE | ID: mdl-12611264

ABSTRACT

A chitinase-producing bacterium, designated WS7b, was isolated from a soil sample obtained from a black-pepper plantation on Bangka Island, Indonesia. Fatty-acid methyl-ester analysis indicated that the isolate was Aeromonas caviae. A chitinase gene from WS7b was cloned in a pUC19-based plasmid vector, but without its natural promoter. The complete nucleotide sequence of the gene was determined, and the structural gene consisted of a 2748-bp region encoding 864 amino acids. DNA sequence analysis indicated that the gene had been cloned without its promoter, and this was confirmed by chitinase-plate assay of the truncated version of the gene in Escherichia coli. The chitinase gene product showed amino-acid sequence similarity to chiA from A. caviae. Chitinase enzyme activity was determined spectrophotometrically, using colloidal chitin azure as substrate for extracellular and intracellular fractions. The ability of the chitinase cloned in E. coli to hydrolyze chitin was less than that of the enzyme in its indigenous host.


Subject(s)
Aeromonas/enzymology , Aeromonas/genetics , Chitinases/biosynthesis , Chitinases/genetics , Aeromonas/chemistry , Amino Acid Sequence , Base Sequence , Cells, Cultured , Chitinases/chemistry , Cloning, Molecular , Enzyme Activation , Escherichia coli/chemistry , Escherichia coli/enzymology , Escherichia coli/genetics , Gene Expression Regulation, Bacterial , Gene Expression Regulation, Enzymologic , Molecular Sequence Data , Piper nigrum/microbiology , Recombinant Proteins/biosynthesis , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Sequence Analysis, DNA , Sequence Analysis, Protein , Soil Microbiology , Species Specificity , Transformation, Genetic
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