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Two pairs of new isobenzofuranone derivative enantiomers, (±)-penicifurans E (1) and (±)-penicifurans F (2), together with four know compounds (3–6) were isolated from the solid fermentation of Penicillium canescens DWS225. The structures of these enantiomers were elucidated by extensive NMR spectroscopic data, and their absolute configurations were assigned by the experimental and calculated ECD data. The neuroprotective effects of all the isolates against oxygen-glucose deprivation/reperfusion injury in pheochromocytoma-12 cells (PC12) were investigated. [ABSTRACT FROM AUTHOR]

Xylanases are used in several industrial applications, such as feed additives, the bleaching of pulp and paper, and the production of bread, food, and drinks. Xylanases are required to remain active after heat treatment at 80–90 °C for 30 s to several minutes due to the conditions of feed pelleting. Also, xylanases need to be active at 60–70 °C for several hours while bleaching of pulp and paper or manufacturing of bread, food, and drinks is performed. Xylanases of the glycoside hydrolase family GH10 are good candidates for application in such processes because of their high thermostability and, in particular, as feed additives because of their insensitivity to protein inhibitors in cereal feeds. In the study, the thermostability of GH10 xylanase E from Penicillium canescens was improved to reach a half-inactivation period of 2 min at 80 °C compared to 21 s for the wild-type enzyme (WT). Enzymatic activity was increased by 22–48 % at 40–70 °C, which improved the action of the enzyme as a feed additive in the gastric system of animals and during bleaching of pulp and paper. Molecular dynamics simulations demonstrated lower flexibility of the tertiary structure of the engineered enzyme at elevated temperatures compared to WT. The residues W113, Q116, W313, and W321 in the (−1) and (−2) subsites for the substrate binding were less flexible. In the simulations, the engineered enzyme had a comparable content of α-helixes, 3 10 -helixes, β-sheets, and β-bridges as WT, but a lower content of coils and a higher content of β-turns. [Display omitted] • Thermostability was improved by six times to reach t 1/2 of 2 min at 80 °C. • Enzymatic activity was increased by 22–48 % at 40–70 °C. • Stability of active center cleft and surface loops and α-helixes was increased. [ABSTRACT FROM AUTHOR]

The interest in peroxidases of the basidiomycete secreted enzyme complex is due to their wide substrate specificity and the ability of these enzymes to participate in the biodegradation of such difficult to degrade biopolymers as lignin. However, due to the difficulty of isolating these enzymes from native sources, their study is difficult. In this work, expression vectors were created that carried the sequence encoding the T. hirsuta LE-BIN072 versatile peroxidase VP2, which was transformed into the genome of the P. canescens strain. Screening of transformants showed the presence of peroxidase activity up to 1 U/mL. Fragments of the target protein in the culture liquids of the selected transformants were identified by mass spectrometric analysis. A new strain, P. canescens pVP2D-6, a producer of the recombinant versatile peroxidase VP2 of T. hirsuta LE-BIN072, was obtained for the first time, and the ability of the enzyme complex secreted by it to modify alkaline lignin was shown. [ABSTRACT FROM AUTHOR]

Objective(s): Salvia abrotanoides is considered as a new source of tanshinone-producing plants in Iran. Symbiosis of endophytic fungi with their host plants is an effective tool to promote the growth and secondary metabolism of medicinal herbs. Therefore, using endophytic fungi as a biotic elicitor is a proper solution to increase the yield of plant products. Materials and Methods: In this study, some endophytic fungi were first isolated from the root of S. abrotanoides, then two of them (Penicillium canescens and Talaromyces sp.) were co-cultivated with the sterile seedling of S. abrotanoides in pot culture. After proving the colonization of these fungi in the root tissues by microscopic studies, their effects on the production of critical medicinal compounds such as tanshinones and phenolic acids were investigated in the vegetation stage (120 days). Results: Our results showed that the content of cryptotanshinone (Cry) and tanshinone IIA (T-IIA) in plants inoculated with P. canescens increased by 77.00% and 19.64%, respectively, compared with non-inoculated plants (control). The contents of mentioned compounds in plants inoculated with Talaromyces sp. increased by 50.00% and 23.00%, respectively. In this case, in plants inoculated with P. canescens, it was found that the level of caffeic acid, rosmarinic acid, and its PAL enzyme activity increased by 64.00%, 69.00%, and 50.00%, respectively, compared with the control.Conclusion: Endophytic fungi have specific modes of action and the ability to provide multiple benefits. Each of the two strains is a highly considerable microbial resource for the growth and accumulation of active compounds of S. abrotanoides.

Objective(s): Salvia abrotanoides is considered as a new source of tanshinone-producing plants in Iran. Symbiosis of endophytic fungi with their host plants is an effective tool to promote the growth and secondary metabolism of medicinal herbs. Therefore, using endophytic fungi as a biotic elicitor is a proper solution to increase the yield of plant products. Materials and Methods: In this study, some endophytic fungi were first isolated from the root of S. abrotanoides, then two of them (Penicillium canescens and Talaromyces sp.) were co-cultivated with the sterile seedling of S. abrotanoides in pot culture. After proving the colonization of these fungi in the root tissues by microscopic studies, their effects on the production of critical medicinal compounds such as tanshinones and phenolic acids were investigated in the vegetation stage (120 days). Results: Our results showed that the content of cryptotanshinone (Cry) and tanshinone IIA (T-IIA) in plants inoculated with P. canescens increased by 77.00% and 19.64%, respectively, compared with non-inoculated plants (control). The contents of mentioned compounds in plants inoculated with Talaromyces sp. increased by 50.00% and 23.00%, respectively. In this case, in plants inoculated with P. canescens, it was found that the level of caffeic acid, rosmarinic acid, and its PAL enzyme activity increased by 64.00%, 69.00%, and 50.00%, respectively, compared with the control. Conclusion: Endophytic fungi have specific modes of action and the ability to provide multiple benefits. Each of the two strains is a highly considerable microbial resource for the growth and accumulation of active compounds of S. abrotanoides. [ABSTRACT FROM AUTHOR]

Two undescribed phenylacetate derivatives (compounds 1 and 2) with a known analog were isolated from a soil-derived fungus Penicillium canescens through the “one strain-many compounds” method. The new structures were assigned using extensive 1D and 2D NMR spectra, high-resolution electrospray ionization mass spectrometry, and the comparison of coupling cleavages of known compounds, which are two pairs of racemic mixtures of aromatic polyketides with a terminal butan-2,3-diol group. In the bioassay, the biological screening signifies no cytotoxic activities against several human cancer cell lines (HL-60, A549, SMMC-7721, MCF-7, and SW480) at a concentration of 40.0 µM.

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FPAses have been isolated and studied from psychrotolerant yeast Rhodotorula mucilaginosa BPT1, Penicillium canescens BPF4 and Pseudogymnoascus roseus BPF6. BPT1 showed 100% activity at 4ºC, 30ºC and 50ºC, while that from BPF4 and BPF6 showed maximal activity at 60ºC and 40ºC respectively. The enzyme from BPT1 showed three peak activities, BPF4 and BPF6 showed single peak activity. While BPT1 FPAse showed 100% activity at low temperature i.e. 4ºC, rendering it very useful enzyme. The FPAses from both the other fungi also showed more than 60% residual activity at cold temperatures. The cold-activity of the enzymes makes them potential for application in simultaneous saccharification and fermentation and other industries especially food processing ones. [ABSTRACT FROM AUTHOR]

Abstract Background Recombinant carbohydrases genes are used to produce transgenic woody plants with improved phenotypic traits. However, cultivation of such plants in open field is challenging due to a number of problems. Therefore, additional research is needed to alleviate them. Results Results of successful cultivation of the transgenic aspens (Populus tremula) carrying the recombinant xyloglucanase gene (sp-Xeg) from Penicillium canescens in semi-natural conditions are reported in this paper for the first time. Change of carbohydrate composition of wood was observed in transgenic aspens carrying the sp-Xeg gene. The transformed transgenic line Xeg-2-1b demonstrated accelerated growth and increased content of cellulose in wood of trees growing in both greenhouse and outside in comparison with the control untransformed line Pt. The accelerated growth was observed also in the transgenic line Xeg-1-1c. Thicker cell-wall and longer xylem fiber were also observed in both these transgenic lines. Undescribed earlier considerable reduction in the wood decomposition rate of the transgenic aspen stems was also revealed for the transformed transgenic lines. The decomposition rate was approximately twice as lower for the transgenic line Xeg-2-3b in comparison with the control untransformed line Pt. Conclusion A direct dependence of the phenotypic and biochemical traits on the expression of the recombinant gene sp-Xeg was demonstrated. The higher was the level of the sp-Xeg gene expression, the more pronounced were changes in the phenotypic and biochemical traits. All lines showed phenotypic changes in the leave traits. Our results showed that the plants carrying the recombinant sp-Xeg gene do not demonstrate a decrease in growth parameters in semi-natural conditions. In some transgenic lines, a change in the carbohydrate composition of the wood, an increase in the cell wall thickness, and a decrease in the rate of decomposition of wood were observed.

Investigations of the influence of chemical and physical factors on the conformational and functional properties of enzymes make a significant contribution to the study of the mechanism of action of industrially important proteins. The aim of the work was to evaluate the effect of chemical reagents and UV irradiation on the catalytic properties of Penicillium canescens α-galactosidase. Enzyme activity was assessed with p-nitrophenyl-α-D-galactopyranoside. Studies of the functionally active glycosidase groups were carried out on the basis of inhibitory and kinetic analysis using Dixon and Luinuiver-Burke methods with help of specific chemical reagents. A significant decrease in the activity of α-galactosidase in the presence of carbodiimi­des, diethylpyrocarbonate, the reagents on sulfhydryl groups was shown. A UV-induced decrease in enzyme activi­ty in the dose range of 900-7200 J/m2 was noted. Based on the data obtained, the imidazole group of histidine, carboxyl groups of C-terminal amino acids and the SH-groups of cysteine are assumed to play an important role in the manifestation of the activity of P. canescens α-galactosidase.

Background: Recombinant carbohydrases genes are used to produce transgenic woody plants with improved phenotypic traits. However, cultivation of such plants in open field is challenging due to a number of problems. Therefore, additional research is needed to alleviate them. Results: Results of successful cultivation of the transgenic aspens (Populus tremula) carrying the recombinant xyloglucanase gene (sp-Xeg) from Penicillium canescens in semi-natural conditions are reported in this paper for the first time. Change of carbohydrate composition of wood was observed in transgenic aspens carrying the sp-Xeg gene. The transformed transgenic line Xeg-2-1b demonstrated accelerated growth and increased content of cellulose in wood of trees growing in both greenhouse and outside in comparison with the control untransformed line Pt. The accelerated growth was observed also in the transgenic line Xeg-1-1c. Thicker cell-wall and longer xylem fiber were also observed in both these transgenic lines. Undescribed earlier considerable reduction in the wood decomposition rate of the transgenic aspen stems was also revealed for the transformed transgenic lines. The decomposition rate was approximately twice as lower for the transgenic line Xeg-2-3b in comparison with the control untransformed line Pt. Conclusion: A direct dependence of the phenotypic and biochemical traits on the expression of the recombinant gene sp-Xeg was demonstrated. The higher was the level of the sp-Xeg gene expression, the more pronounced were changes in the phenotypic and biochemical traits. All lines showed phenotypic changes in the leave traits. Our results showed that the plants carrying the recombinant sp-Xeg gene do not demonstrate a decrease in growth parameters in semi-natural conditions. In some transgenic lines, a change in the carbohydrate composition of the wood, an increase in the cell wall thickness, and a decrease in the rate of decomposition of wood were observed. [ABSTRACT FROM AUTHOR]

A new isopentylated dibenzodioxocinone, canescenin A (1), and a new isopentylated pyran-3,5-dione derivative, canescenin B (2), were isolated from an extract of the deep-sea-derived fungus Penicillium canescens SCSIO z053. Their structures were elucidated by spectroscopic analysis. It was rare to obtain pyran-3,5-dione derivatives from nature. Antibacterial, cytotoxic, and antiviral activities of 1 and 2 were also evaluated. [ABSTRACT FROM AUTHOR]

Laccases (EC 1.10.3.2) are multicopper polyphenol oxidases found in various organisms, in particular, in fungi. Fungal laccases are encoded by multigene families, which can contain up to 17 genes. However, not all isozymes can be obtained from native producers. Previous studies have shown that the filamentous fungus Penicillium canescens is a promising object for the heterologous expression of various laccase isozymes of Trametes hirsuta 072. In this work, the cultivation conditions of P. canescens strains, recombinant producers of T. hirsuta heterologous minor laccase, are optimized. The optimization of the rLacD and rLacF purification method increased their yield and specific activity of rLacD. In addition, the melting points of minor laccase isoenzymes are measured and the glycosylation of isoenzymes is studied. [ABSTRACT FROM AUTHOR]

The aim of this work was the study of native and galactosidases from Penicillium canescens under denaturing conditions caused by guanidine hydrochloride. Calculation of kinetics and constants of enzymes inactivation was carried out on using experimental kinetic curves of enzyme denaturation. We observed significant differences in the kinetics of inactivation of native and deglycosylated α-galactosidases from P. canescens caused by guanidine hydrochloride. Native enzyme was stable within the selected range of guanidine hydrochloride concentrations (from 0.1 to 3.0 M), retaining no less than 50% of the initial enzyme activity for 3 days. Deglycosylated enzyme preparations were less stable and they lost their activity within 5–30 minutes, when they were treated with guanidine hydrochloride in concentrations above 1 M. Dissociation rate constant of native and deglycosylated forms of the enzyme differed by 10 to 100 folds. It was shown that subunit interactions play a major role in the process of inactivation of the enzyme, and the carbohydrate component is essential for stabilizing of subunit bonds and maintaining conformational stability of the enzyme under denaturing conditions of chemical agents.

A novel exo-arabinase (GH93, exo-ABN) enzyme produced by the ascomycete Penicillium canescens has been studied. Cloning of the abn1 gene coding for exo-ABN into the recipient P. canescens strain RN3-11-7 yielded recombinant producing strains characterized by a high yield of extracellular exo- ABN production (20-30% of the total amount of extracellular protein). Chromatographic purification yielded a homogenous exo-ABN with a molecular weight of 47 kDa, as shown by SDS-PAGE. The enzyme showed high specific activity towards linear arabinan (117 U/mg) and low specific activity towards branched arabinan and arabinoxylan (4-5 U/mg) and para-nitrophenyl-α-L-arabinofuranoside (0.3 U/mg), whereas arabinogalactan and para-nitrophenyl-α-L-arabinopyranoside, the substrates that contained the pyranose form of arabinose, were not hydrolyzed. Arabinohexaose was the major product of linear arabinan hydrolysis. Exo-ABN had a pH optimum at 5.0 and a temperature optimum at 60°C. The enzyme was stable in a broad pH range (4.0-7.0) and upon heating to 50°C during 180 min. Extensive hydrolysis of linear and branched arabinans by exo- and endo-arabinase mixtures, arabinofuranosidase, and arabinofuran-arabinoxylan hydrolase has been performed. The degree of substrate conversion amounted to 67 and 83% of the maximal possible value, respectively. [ABSTRACT FROM AUTHOR]

New recombinant strains based on the lower fungus Penicillium canescens are engineered to produce an extracellular enzyme complex that contains a homologous endo-1,4-β-xylanase E (XylE, EC 3.2.1.8). Expression of the gene encoding XylE is controlled by the promoter of the xylA gene, which encodes endo- 1,4-β-xylanase A. Comparative analysis of enzyme preparations (EPs) isolated from the culture liquid of the host strain (Penicillium canescens RN3-11-7) and the new recombinant P. canescens strains of the XylE series is performed. The specific activity of the EPs against a specific substrate (birch glucuronoxylan) is studied, and the qualitative and quantitative composition of the new EPs XylE-B5 and XylE-C1, as well as the RN3 EP from the host strain, is determined. The decrease in the reduced viscosity of native (not subjected to thermal inactivation) aqueous extracts of rye treated with XylE-B5 EP was double that in the case of treatment with RN3 EP, due to high content of inhibition-resistant XylE in the new EPs. [ABSTRACT FROM AUTHOR]

The effect of the glycosylation inhibitors (tunicamycin and 2-deoxy-D-glucose) on the activity, stabili­ty and production of fungal glycosidases has been studied. It was shown that inhibition of N-glycosylation sites did not affect the secretion of Aspergillus niger α-galactosidase, however reduced yield of Cladosporium cladosporioides and Penicillium canescens α-galactosidases. Changes in the level of O-glycosylation resulted in a significant reduction in the activity and stability of α-galactosidases of all three producers tested. Activity of the modified enzymes was significantly lower than that of the native ones, and was 2.6 and 0.33 U/mg for A. niger α-galactosidase, 3.3 and 32.5 U/mg for C. cladosporioides α-galactosidase, 11.66 and 31.1 U/mg for P. canescens α-galactosidase, respectively. A. niger α-galactosidase completely lost activity during purification and storage. The decrease of thermal stability at 55 °C by 20% was shown for C. cladosporioides and P. canescens α-galactosidases. It was also noted that O-deglycosylation led to a decrease in resistance of these enzymes to the action of proteases.

In order to investigate factors affecting the thermostability of GH10 xylanase A from Penicillium canescens (PcXylA) and to obtain its more stable variant, the wild-type (wt) enzyme and its mutant forms, carrying single amino acid substitutions, were cloned and expressed in Penicillium verruculosum B1-537 ( niaD- ) auxotrophic strain under the control of the cbh1 gene promoter. The recombinant PcXylA-wt and I6V, I6L, L18F, N77D, Y125R, H191R, S246P, A293P mutants were successfully expressed and purified for characterization. The mutations did not affect the enzyme specific activity against xylan from wheat as well as its pH-optimum of activity. One mutant (L18F) displayed a higher thermostability relative to the wild-type enzyme; its half-life time at 50–60 °C was 2–2.5–fold longer than that for the PcXylA-wt, and the melting temperature was 60.0 and 56.1 °C, respectively. Most of other mutations led to decrease in the enzyme thermostability. This study, together with data of other researchers, suggests that multiple mutations should be introduced into GH10 xylanases in order to dramatically improve their stability. [ABSTRACT FROM AUTHOR]

A novel biotechnology approach by combining deacetylation biocatalysis with elicitation of immobilized Penicillium canescens ( IPC) in Astragalus membranaceus hairy root cultures ( AMHRCs) was proposed for the elevated production of astragaloside IV ( AG IV). The highest AG IV accumulation was achieved in 36-day-old AMHRCs co-cultured with IPC for 60 h, which resulted in the enhanced production of AG IV by 14.59-fold in comparison with that in control (0.193 ± 0.007 mg/g DW). Meanwhile, AG IV precursors were almost transformed to AG IV by IPC deacetylation. Moreover, expression of genes involved in AG IV biosynthetic pathway was significantly up-regulated in response to IPC elicitation. Also, FTIR and SEM showed that cell wall lignification was enhanced following IPC treatment and root surface was likely to be IPC deacetylation site. Overall, dual roles of IPC (biocatalyst and elicitor) offered an effective and sustainable way for the mass production of AG IV in AMHRCs. [ABSTRACT FROM AUTHOR]

Microbial aspects of endo-β-1,4-xylanase production in solid-state fermentation by Penicillia: the case of Penicillium canescens. Production of xylanases by Penicillium canescens 10-10c is the research object in Walloon Center of Industrial Biology. Previous works used submerged or liquid fermentation. The actual works are oriented more and more towards solid fermentation from agricultural or agro-alimentary residues. In addition to the valorization of these residues, solid-state fermentation reaches an increasingly significant interest in various other fields like the biological breakdown of the solid residues, the bioremediation of the organic pollutants in the grounds and the reduction of the air pollution by the biofiltration. Xylanase is an industrial enzyme used in general in extraction and clarification processes. P. canescens can produce an activity of it, particularly in its balanced forms of xylanases, beta-xylosidase and arabinosidase, and not contaminated by cellulolytic and amylolytic activities. It is a hyper producing strain of xylanase. The production rate is one of the highest in literature (535 U.ml-1 and 9,632 U.g-1 in Erlenmeyer flasks, in submerged and solid state fermentation, respectively). The biobleaching activity of the cellulose pulp by the purified enzyme is higher than a commercial preparation of xylanases from Trichoderma longibrachiatum used industrially. It has a complete hydrolysis degree of 40% (on glucuronoxylan) and 35% (on arabinoxylan) at 55°C and at pH of 5.9. These characteristics lead to many industrial applications of this enzyme. That is why the optimization of its production by the solid-state fermentation at the laboratory scale in order to define a policy for the industrial transposition later is carried out. This article presents a summary of the scientific literature on this subject.

Two undescribed polyketides canecines A-B, one unreported cyclopentenone canecine C, together with 12 known compounds were isolated from an extract of the fungus Penicillium canescens DJJ-1. Their structures were elucidated by detailed analysis of spectroscopic data, NMR calculations with d J -DP4 or DP4+, and their absolute configurations were further determined by quantum chemical calculations of ECD spectra or X-crystallography. Canecine A was a grisan polyketide featuring a dimethyltetrahydro-4 H -furo[2,3- b ]pyran. Canecine A exhibited significant inhibitory activity against Candida albicans with an MIC value of 1 μg/mL and showed inhibitory effect on nitric oxide production in LPS-activated RAW264.7 macrophages. These results enrich the structural diversities of polyketides from endophytic fungi. Polyketides with antimicrobial activities from Penicillium canescens DJJ-1 of Aconitum brevicalcaratum Diels (Ranunculaceae). [Display omitted] • Three undescribed polyketides were isolated from Penicillium canescens DJJ-1. • One compound showed antimicrobial activities. • One compound showed inhibitory effects on LPS-induced NO production. [ABSTRACT FROM AUTHOR]

Objectives: Salvia abrotanoides is considered as a new source of tanshinone-producing plants in Iran. Symbiosis of endophytic fungi with their host plants is an effective tool to promote the growth and secondary metabolism of medicinal herbs. Therefore, using endophytic fungi as a biotic elicitor is a proper solution to increase the yield of plant products., Materials and Methods: In this study, some endophytic fungi were first isolated from the root of S. abrotanoides , then two of them ( Penicillium canescens and Talaromyces sp.) were co-cultivated with the sterile seedling of S. abrotanoides in pot culture. After proving the colonization of these fungi in the root tissues by microscopic studies, their effects on the production of critical medicinal compounds such as tanshinones and phenolic acids were investigated in the vegetation stage (120 days)., Results: Our results showed that the content of cryptotanshinone (Cry) and tanshinone IIA (T-IIA) in plants inoculated with P. canescens increased by 77.00% and 19.64%, respectively, compared with non-inoculated plants (control). The contents of mentioned compounds in plants inoculated with Talaromyces sp . increased by 50.00% and 23.00%, respectively. In this case, in plants inoculated with P. canescens , it was found that the level of caffeic acid, rosmarinic acid, and its PAL enzyme activity increased by 64.00%, 69.00%, and 50.00%, respectively, compared with the control., Conclusion: Endophytic fungi have specific modes of action and the ability to provide multiple benefits. Each of the two strains is a highly considerable microbial resource for the growth and accumulation of active compounds of S. abrotanoides., Competing Interests: The authors declare that they have no competing interests.

The producer of fungal penicillopepsin, an aspartate protease, has been created by genetic engineering. The biochemical and physicochemical properties of the penicillopepsin enzyme preparation obtained from the culture liquid of the producer were studied. Properties of the new enzyme preparation and the commercially available aspergillopepsin were compared. Their proteolytic activities were found to be 670-680 U/g of the preparation. The soluble protein yield upon the wheat flour hydrolysis with penicillopepsin was 2.7 times higher than with aspergillopepsin. It is probably caused by the presence of the xylanase activity in the penicillopepsin preparation. [ABSTRACT FROM AUTHOR]

Two xylanases (XylA and XylE) of glycoside hydrolase family 10 are isolated from an enzyme preparation produced by Penicillium canescens fungi. The kinetics of the hydrolysis of glucuronoxylan and arabinoxylan by the purified enzymes and the effect of proteinaceous (XIP-like) inhibitors from rye on the viscometric activity of the xylanases are studied. XylA provides a more complete conversion of glucuronoxylan than XylE, while XylE is more effective in the arabinoxylan hydrolysis. Unlike XylA, XylE is resistant to the proteinaceous inhibitors from rye-this property is rarely found in the enzymes of family 10. Thus, XylE is a promising enzyme for use as a cereal feed additive, while XylA may potentially be used for the biobleaching of cellulose from hardwoods, which contain glucuronoxylan as one of the major components. [ABSTRACT FROM AUTHOR]

Recombinant strains of Penicillium canescens producing homologous pectin lyase A and heterologous endo-1,5-α-arabinase A and endo-1,4-α-polygalacturonase, as well as enzymes of the host strain (α-L-arabinofuranosidases, xylanases, and others), were obtained by genetic engineering. The enzyme preparations (EPs) obtained from the cultural medium of recombinant P. canescens strains efficiently hydrolyzed raw plant material with a high content of pectin compounds. It was shown that the yield of reducing sugars and arabinose increased 16 and 22% in comparison with the control EP based on the host strain when one of the obtained EPs was used for beet pulp hydrolysis. It was established that the most active EP consisted of pectin lyase (10%), endo-1,5-arabinase (26%),α-L-arabinofuranosidase and arabinoxylan-arabinofuranohydrolase (12%), and xylanase (10%). The activities of pectin lyase, polygalacturonase, and arabinase of the EP in reactions with various substrates were determined. The specificity, pH and T-optima, and thermal stability of the homogenous recombinant endo-1,5-α-arabinase were investigated. The kinetic parameters ( K, k) of the linear arabinan hydrolysis were determined. [ABSTRACT FROM AUTHOR]

Penicillium canescens is a filamentous fungus that normally does not secrete notable levels of cellulase activity. Cellobiohydrolase I of P. canescens (PcCel7A) was homologously cloned into a host strain RN3-11-7 ( niaD- ) and then expressed under the control of a strong xylA promoter. Using three steps of chromatography, PcCel7A was purified. The enzyme displayed maximum activity at pH 4.0–4.5. PcCel7A was stable at 50 °C and pH 4.5 at least for 3 h, while at 60 °C it lost 45% of activity after 30 min of incubation. When equalized by protein concentration, PcCel7A demonstrated a higher performance in prolonged hydrolysis of Avicel and milled aspen wood than CBH I (Cel7A) from Trichoderma reesei , the most industrially utilized cellulase at this moment. The high catalytic efficiency of the PcCel7A makes it a potential candidate for industrial applications. [ABSTRACT FROM AUTHOR]

Highlights: [•] The novel biotransformation was environmentally friendly and high-efficiency. [•] Deacetylation of the fungal endophyte was significant. [•] The fungal endophyte was firstly isolated from pigeon pea. [•] Content of astragaloside IV was 5.51-fold to untreated one after biotransformation. [•] An alternative for the production of astragaloside IV in commercial process. [ABSTRACT FROM AUTHOR]