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The study shows that La2O3 at a concentration of 30-450 mg.L-1 could inhibit the growth of S. sclerotiorum in both solid and liquid media and the inhibition effect was increased with its increasing concentration. The activity of pectinase produced by S. sclerotiorum in liquid medium was also increased with increasing La2O3 concentration.
Production of an extracellular pectinase by wood-rot fungi of the genus Bjerkandera and Coriolus was studied. The active producers B. adusta 40 and C. versicolor 24 were selected. The dynamics of production of pectinase and effects of temperature, initial pH, humidity of the medium and addition of nitrogen sources on the biosynthesis of pectinase were studied.
This study describes an effective method of in situ RT-PCR (RT-ISPCR) that was developed to localize gene expression in plant tissues. This RT-PCR technique was performed on sectioned tissues of female buds of the cucumber GY3 inbred line. The CUS1 gene, encoding the MADS-box type (agamus-like) protein, the expression pattern of which was described earlier, was used as a marker gene for optimisation of steps in the in situ RT-PCR inside the cells. For the identification of RT-PCR products inside the cells of the female buds, they were fixed in FAA solution, embedded in Paraplast Plus and cut into 7 microm thick sections which were dewaxed by immersion in HistoClear and dehydrated with ethanol. They were washed in water, then in 0.02M HCl, 2xSSC and PBS buffer. In the next step of tissue pretreatment, the sections were digested with 1% pectinase. As shown, the pectinase treatment proved to be a crucial step in the tissue preparation procedure to get successful RT-PCR products. After washing in PBS buffer, the sections were digested with protease K followed by incubation with RNase-free DNase I, and subsequently washed in 2xSSC, 1xSSC and 0.5xSSC and finally in DEPC-treated water. Then the sections were covered with 50 microl of the RT-PCR reaction mixture supplemented with 0.5 microM digoxigenin dUTP and sealed with a coverslip. After amplification in situ the PCR products were identified with anti-digoxigenin antibody (Roche Molecular Biochemicals), conjugated with alkaline phosphatase. The data obtained showed that specific signals reflecting CUS1 gene expression were detected in the female flower buds of cucumber. The specificity of the in situ RT-PCR protocol was confirmed by dot blot hybridization of RT-PCR products with CUS1 cDNA probe.
Effect of commercial pectinase and cellulase addition on in vitro digestibility of two common bean (Phaseolus vulgaris) varieties, black (Brunca) and red (Chirripó), was measured. Constant conditions of pH (6.3-6.4), time (60 min), and temperature (40 degrees C) were held, and three enzyme concentrations were tested: 0.25%, 0.5% and 1.0% m/m. In vitro digestibility increases for black beans were 6.9%; 9.5% and 12.3% (p < 0.05), and for red beans were 8.9%; 10.2% and 12.9% (p < 0.05), with increasing pectinase concentration. Effects of cellulase were dependent upon both, enzyme concentration and bean variety. In vitro digestibility of red beans increased by 5.7%; 9.2% and 12.0% with increasing cellulase concentration; digestibility of black beans increased by less than 5%. No significant difference (p > 0.05) in general acceptance of enzyme treated beans (black or red) or nontreated beans was noted.
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In rice, nodule like structures were formed by inoculation of A. caulinodans combined with growth regulators and enzymes. Among the treatments, combination of cell wall degrading enzyme mixture and NAA with A. caulinodans induced more number of paranodules in rice. Total nitrogen content also increased in treated plants compared to uninoculated control.
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We studied the changes in lectin activity in tobacco leaf disc and potato tubers treated with polysaccharides (chitosan, glucomannan, and dextran sulfate), enzymes (cellulase and pectinase), or monosaccharides (glucose and glucosamine). All studied substances changed lectin activity to a certain extent(significantly or as a trend). The number of membrane lectins in the chloroplasts (tobacco leaf discs) usually considerably decreased immediately after the treatment (1-2 days) but increased later (2-4 days). Generally, an increased lectin activity predominated in potato tubers treated with the inducers. The enzymes increased lectin activity during the whole observation period (5 days). A pronounced antiviral activity was observed in the hypersensitive tobacco-tobacco mosaic virus system only after treatment with chitosan and glucomannan.
The extraction technology of flavonoids from Ginkgo biloba leaves was studied in this paper. When the crude leaves used the cellulase enzyme pretreatment before extraction process, the extraction yield of total flavone was up to 2.01%. The extraction conditions were also determined experimentally as following: concentration of enzyme in the liquor being 0.125 g/L, mixture ratio between enzyme and substrate being 1:1200, treating 2 hours, at 45 degrees C, under natural pH value.
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Penicillium griseoroseum, a deuteromycete fungus producer of pectinolytic enzymes, was transformed with a gene encoding for green fluorescent protein (GFP). The selection of transformants was based on the homologous nitrate reductase gene (niaD). Protoplasts of a P. griseoroseum Nia mutant (PG63) were co-transformed with the plasmids pNPG1 and pAN52-1-GFP. The plasmid pNPG-1 carries the homologous niaD gene and pAN52-1-GFP carries the SGFP-TYG version of GFP. The highest transformation efficiency (102 transformants/mug of pNPG1) resulted from the utilization of equimolar amounts of transforming and co-transforming vectors. Analysis of pAN52-1-GFP insertions into the genomic DNA of the transformants revealed single and multiple copy integrations. The transformants possessing a single copy of the gfp gene showed a low level of fluorescence, whereas multicopy transformants displayed strong fluorescence under visualization with fluorescent light. The transformants showing high expression of the gfp gene had the normal mycelia pigmentation altered, displaying a bright green-yellowish color, visible with the naked eye on the plates, without the aid of any kind of fluorescent light or special filter set.
Using Aspergillus niger AN01 as original strain, mutated strain Aspergillus niger AN03 was obtained by N+ implantation. The results showed that activities of acidic protease, cellulase and pectinase of Aspergillus niger were raised from 71.6U/g, 141.7U/g and 264.8U/g to 996.5U/g, 940.4U/g and 906.5U/g respectively. Characteristics of enzymes production in the mutant Aspergillus niger AN03 kept stabile by 5 times subculture. In addition, the optimum conditions for enzymes production of Aspergillus niger AN03 were investigated. The optimum components of medium consisted of bran 105.0g, corn straw 105.0g, bean cake 105.0g, NH4Cl 6.0g, H2O 1000mL. The optimum fermentation condition was incubated for 4d in the condition of pH 5.0 and temperature 30 degrees C.
The effects of commercial and laboratory preparations were compared in the course of treatment of components of compound fodder. The most potent preparations were selected for the treatment of soybean flower, sunflower meal, and wheat and barley flour. Preparation 181-1008, which had a high proteinase activity, provided the highest yield of protein from soybean flour and sunflower meal. Preparations aGA, AG20X, and VR, characterized by high activities of pectinase and alpha-galactosidase, as well as laboratory preparation B2000Mix with a high activity of alpha-galactosidase, provided the highest yield of sugars from soybean flour. Preparations with high alpha-galactosidase activity were the most potent in hydrolyzing soluble carbohydrates from soybean flour. The highest yield of reducing sugars was observed after treatment of wheat and barley flour with preparations B2000Mix and aGa. Xylanase activity of these preparations was lower than that of preparations 3.130.2 and TG20X. Preparations 3.130.2 and TG20X were the most potent in hydrolyzing wheat middlings.
The results of the enzymatic hydrolysis of pectin, hemicellulose and cellulose in the biomass of sweet sorghum (Sorghum vulgare var. saccharatum, L.) are reported. Some commercial enzymatic preparations were used: Maxazym CL 2000 (with prevailing cellulase activity), Rapidase C 80 (with prevailing pectinase activity) Rohament PC (mainly with pectinase and cellulase activities) and Rohament O (mainly with pectinase and hemicellulase activities). The treatment with Rohament PC, Rohament O and Rapidase C 80 gives an increase of the glucose content higher than the effect induced by Maxazym CL 2000. On the other hand, the cellulase and pectinase combined treatment (Maxazym CL 2000 + Rapidase C 80 or Maxazym CL 2000 + Rohament O) shows a good synergistic effect in the degradation of the plant cell wall cellulosic material.
From conidia of 4 different auxotrophic A. niger strains 400 spontaneous revertants (100 from each strain) were obtained, and in one case additionally 100 revertants induced by mutagens (UV+NTG). The revertants showed a considerable differentiation with regard to the total pectinolytic activity. Its highest increase occurred in revertants originating from auxotrophs greatly predisposed to synthesize pectinases. In the case of revertants induced by mutagenes an increase in the frequency of their formation was observed, as well as an increased participation of revertants with higher pectinolytic activity compared to both their initial auxotrophic and prototrophic strain.