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Most traditional injection-production optimization methods that treat the entire oil reservoir as a whole require re-optimization when facing new reservoirs, which is not only time-consuming but also does not make full use of historical experience information. This study decomposes the reservoir into independent basic production units to increase sample size and diversity and utilizes image enhancement techniques to augment the number of samples. Two frameworks based on convolutional neural networks (CNNs) are employed to recommend optimal control strategies for inputted well groups. Framework 1 uses bottom hole pressure (BHP) as a control variable and trains a CNN with optimal BHP obtained by reinforcement learning algorithms as labels. Framework 2 saves BHP and corresponding oil well revenue (NPV) during reinforcement learning optimization and trains a CNN with well groups and BHP as features and NPV as labels. The CNN in this framework is capable of directly outputting the NPV according to control strategies. The particle swarm algorithm (PSO) is used to generate control strategies and call CNN to predict development effects until PSO converges to the optimal production strategy. The experimental results demonstrate that the CNN-based frameworks outperform the traditional PSO-based methods in terms of accuracy and computational efficiency. Framework 1 achieves an output accuracy of 87% for predicting the optimal BHP for new well groups, while Framework 2 achieves an accuracy of 78%. Both frameworks exhibit fast running times, with each iteration taking less than 1 s. This study provides a more effective and accurate method for optimizing oil well production in oil reservoirs by decomposing oil reservoirs into independent units and using CNN to construct an algorithm framework, which is of great significance for the real-time optimization and control of oil wells in oil fields.

To determine the accuracy, repeatability, and reproducibility of magnetic resonance imaging-based proton density fat fraction (MRI-PDFF) measurements of rotator cuff muscles between two readers and three different scanners.Twenty-seven volunteers underwent serial shoulder MRI examinations of both left and right sides on one 1.5-T MRI scanner and two 3.0-T MRI scanners. Two independent readers measured muscular PDFF of the supraspinatus, infraspinatus/teres minor muscle, and subscapularis. MR spectroscopy-based proton density fat fraction (MRS-PDFF) was regarded as the reference standard for assessing accuracy. A "coffee break" examination method was used to test the repeatability of each scanner. Bland-Altman plots, Pearson correlation, and linear regression analysis were used to assess bias and linearity. The Wilcoxon signed-rank test and Friedman test were applied to evaluate repeatability and reproducibility.MRI-PDFF measurements indicated strong linearity (RMRI-PDFF measurements of rotator cuff muscles were highly accurate, repeatable, and reproducible across different readers and scanners, leading us to the conclusion that PDFF can be a reliable and robust quantitative imaging biomarker for longitudinal or multi-center studies.

Preoperative differentiation between benign lymphoepithelial lesion (BLEL) and mucosa-associated lymphoid tissue lymphoma (MALToma) in the parotid gland is important for treatment decisions. The purpose of this study was to develop and validate a CT-based radiomics nomogram combining radiomics signature and clinical factors for the preoperative differentiation of BLEL from MALToma in the parotid gland.A total of 101 patients with BLEL (n = 46) or MALToma (n = 55) were divided into a training set (n = 70) and validation set (n = 31). Radiomics features were extracted from non-contrast CT images, a radiomics signature was constructed, and a radiomics score (Rad-score) was calculated. Demographics and CT findings were assessed to build a clinical factor model. A radiomics nomogram combining the Rad-score and independent clinical factors was constructed using multivariate logistic regression analysis. The performance levels of the nomogram, radiomics signature, and clinical model were evaluated and validated on the training and validation datasets, and then compared among the three models.Seven features were used to build the radiomics signature. The radiomics nomogram incorporating the clinical factors and radiomics signature showed favorable predictive value for differentiating parotid BLEL from MALToma, with AUCs of 0.983 and 0.950 for the training set and validation set, respectively. Decision curve analysis showed that the nomogram outperformed the clinical factor model in terms of clinical usefulness.The CT-based radiomics nomogram incorporating the Rad-score and clinical factors showed favorable predictive efficacy for differentiating BLEL from MALToma in the parotid gland, and may help in the clinical decision-making process.• Differential diagnosis between BLEL and MALToma in parotid gland is rather difficult by conventional imaging modalities. • A radiomics nomogram integrated with the radiomics signature, demographics, and CT findings facilitates differentiation of BLEL from MALToma with improved diagnostic efficacy.

A novel peroxidase has been isolated from fresh fruiting bodies of the mushroom Pleurotus pulmonarius, with a purification protocol of ion exchange chromatography on DEAE-cellulose, affinity chromatography on ConA-Sepharose, ion exchange chromatography on CM-cellulose, and gel filtration by FPLC on Superdex 75. The peroxidase was unadsorbed on either DEAE-cellulose or ConA-Sepharose, but was adsorbed on CM-cellulose. It exhibited a molecular mass of 55 kDa in gel filtration and also in sodium dodecyl sulfate–polyacrylamide gel electrophoresis, indicating that it is a monomeric protein. It possessed a distinctive N-terminal amino acid sequences from other isolated mushroom peroxidases. The optimal pH and temperature for the enzyme were 4.0 and 70 °C, respectively. All enzyme activity was destroyed after exposured in 100 °C for 10 min. The peroxidase did not exhibit HIV-1 reverse transcriptase inhibitory activity and antifungal activity. The stability against high temperature and extreme pH supported that the enzyme could be a potential peroxidase source for special industrial applications.

A novel lectin (ABL) was purified from the dried fruiting bodies of Agaricus bitorquis. An efficient 3-step purification protocol involved two consecutive steps of ion exchange chromatography on Q-Sepharose and SP-Sepharose and gel filtration by FPLC on Superdex 75. ABL is a monomeric protein with the molecular mass of 27.6 kDa, which is different from other lectins from genus Agaricus. Its N-terminal amino acid sequence is EYTISIRVYQTNPKGFNRPV which is unique and sharing considerably high similarity of other mushroom lectins. The hemagglutinating activity of the lectin was inhibited by inulin. Based on hemagglutination tests, ABL prefers rabbit, human type A, and AB erythrocytes to human type B and O erythrocytes. The lectin inhibits the activity of HIV-1 reverse transcriptase and the proliferation of leukemia cell (L1210) with an IC50 value of 4.69 and 4.97 μM, respectively. Furthermore, ABL demonstrates the highest mitogenic activity with a response of 24177.7 ± 940.6 [3H-methyl] thymidine counts per minute (CPM) at a concentration of 0.91 μM.

A 37.4 kDa acid tolerant lectin was isolated and purified from dried fruiting bodies of Amanita hemibapha var. ochracea designated as AHL. The lectin was not adsorbed on DEAE-cellulose, but rather adsorbed on S-Sepharose and subjected to gel filtration by fast protein liquid chromatography on Superdex 75. The purified lectin was immune from inhibition activities of metal ions. More over, AHL exhibited high agglutination activity on rabbit erythrocytes with accelerating Hg 2+ ions concentration. Partial peptide sequence analysis (VSNNLLTGPKVVR) of this lectin showed relative similarity to phosphoenolpyruvate carboxykinase [ATP]-like protein as predicted from Fragaria vesca subsp. Vesca . Interestingly, AHL displayed a strong affinity toward α-Lactose, making our study the first report associating Amanita species’ lectin specificity for α-Lactose to the best of our knowledge.

We described the purification and characterization of a novel extracellular laccase from the traditional Chinese medicinal mushroom Inonotus baumii with antiproliferative activity. The laccase (IBL) was purified from fermentation broth of I. baumii by employing initial filtration and centrifugation steps, followed by three ion-exchange chromatography steps comprising DEAE-cellulose, CM-cellulose, and Q-Sepharose, and a final gel-filtration step by fast protein liquid chromatography (FPLC) on Superdex 75. The purified enzyme was a monomeric protein with a molecular mass of 66 kDa calculated by FPLC and SDS-PAGE. It possessed an N-terminal amino acid sequence of AIGPVDEV (SPIN: C0HJB2), a temperature optimum of 20 °C, pH optima of 2.4 and 3.2 toward ABTS and guaiacol respectively, and Km values of 1.31 mM and 2.27 mM toward ABTS and guaiacol respectively at pH 2.4 and 30 °C. The ranking of its oxidative activity toward various aromatic substrates was ATBS > guaiacol > 4-methylcatechol > 4-hydroxyindole > catechol > hydroquinone > 2,6-dimethoxy-phenol (19.6%) > pyrogallol > ferulic acid > N, N-dimethyl-1, 4-phenylenediamine. Cu 2+ can enhance the enzyme activity of 10.8–14.6 fold in the ion concentration range of 1.25–10 mM. IBL manifested antiproliferative activities toward HepG2 and L1210 cells with IC 50 values of 2.4 μM and 3.2 μM, respectively, but is devoid of inhibitory activity toward HIV-1 reverse transcriptase.

An acidic α-galactosidase (EC 3.2.1.22) designated as Phaseolus coccineus seeds galactosidase (PCG) was purified from P. coccineus seeds using ion-exchange chromatography on DEAE- and CM-cellulose, Q- and SP-Sepharose and gel filtration on Superdex 75. The molecular weight of PCG was 43 kDa as judged by SDS-PAGE and gel filtration. Two inner peptides of PCG were sequenced by MALDI-TOF-MS. The optimum pH and temperature was 3.0 and 70 °C, respectively but was stable up to 60 °C for 30 min. The enzyme activity was inhibited by NBS signifying the pivotal role played by tryptophan in the catalytic activity of the enzyme. The Km for hydrolysis of pNPGal was 0.0025 mM. Besides hydrolyzing pNPGal, α-galactosidases also hydrolyzed natural substrates such as melibiose, raffinose and stachyose. Hence it can be exploited commercially for improving the nutritional value of soymilk. Thus the PCG has great potential in the feed industries for removal of non-digestible oligosaccharide from legumes.

A novel laccase was purified and characterized from an edible mushroom Russula virescens by using a protocol that comprised ammonium sulfate saturation, ion-exchange chromatography on diethylaminoethyl-cellulose, carboxymethyl-cellulose and quaternary amine-Sepharose, and finally gel filtration by fast protein liquid chromatography on Superdex 75. The laccase was a monomeric protein with a molecular mass of 69 kDa. Its N-terminal amino acid sequence was AIGPTAELVV which demonstrated partial sequence homology to those of previously published laccases. Six peptide sequences of the purified laccase were determined by liquid chromatography and linear ion trap quadrupole mass spectrometry. Its optimum pH and temperature were 2.2 and 60 °C, respectively. The laccase was inhibited by inhibitors and several metal ions including Cu2+ ions. The laccase degraded various phenolic compounds and the Km toward both 2,7-azinobis (3-ethylbenzothia-zolone-6-sulfonic acid) diammonium salt and dimethylphthalate was 0.1 mM. Moreover, the purified laccase decolorizes a large variety of dyes comprising laboratory dyes such as Bromothymol Blue, Eriochrome black T and Malachite Green and textile dyes such as Reactive Brilliant Blue and Reactive Blue R.

A novel lectin was isolated from the dried fruiting bodies of the wild mushroom Paxillus involutus. Isolation was conducted by anion exchange chromatography on DEAE-Cellulose, Q-Sepharose and gel filtration on Superdex 75 using a fast protein liquid chromatography (FPLC) system. This lectin had a molecular mass of 28 kDa and was composed of four identical subunits, each with a molecular mass of 7 kDa. N-terminal amino acid sequence of the P. involutus lectin was determined to be CTCAVFLNNTTVKS, which showed a low level of similarity to mushroom lectin sequences reported previously. The biochemical properties of this lectin were determined, and the hemagglutinating activity was inhibited by inulin and O-Nitrophenyl-β-D-galacto-pyranoside. Additionally, Ca2+, Zn2+, Cd2+, Fe2+, and Al3+ inhibited its hemagglutinating activity, while Cu2+ promoted this activity. This lectin exhibited poor thermostability and was sensitive to HCl, but it had a high tolerance to NaOH exposure. In terms of biological properties, this lectin manifested antiphytovirus activity towards tobacco mosaic virus (TMV) with a 70.61% inhibition at a concentration of 200 µg/mL. This lectin was devoid of inhibitory activities toward pathogenic fungi and HIV-1 reverse transcriptase, and antiproliferative activities were observed in tumor cell lines including lung cancer A-549 and human colon cancer HCT-8 cells.

Auricularia auricula-judae, also known as black wood ear, is one of the most popular edible mushrooms in China. But the confusion about cultivars has limited the development of A. auricula-judae production. In this article, 17 polymorphic SSR markers were cloned and used to differentiate the cultivars of A. auricula-judae. The polymorphism information content (PIC) of these SSR ranged from 0.10 to 0.84, while the average was 0.47. The number of alleles detected for each locus was 2–11, with an average of 4.7 alleles per locus. The dendrogram, based on 17 SSR markers by UPGMA clustering, could differentiate the 16 A. auricula-judae cultivars in this study. In fact, the 16 cultivars analyzed in this study could be efficiently differentiated using a combination of three polymorphic SSR loci with high PIC. The total of 17 polymorphic SSR loci could also be amplified correctly in the A. polytricha strains surveyed. This is the first report on the development of SSR markers in the genus Auricularia.

An antiproliferative ribonuclease with a new N-terminal sequence was purified from fruiting bodies of the edible wild mushroom Russula delica in this study. This novel ribonuclease was unadsorbed on DEAE-cellulose, but absorbed on SP-Sepharose and Q-Sepharose. It had a molecular mass of 14 kDa as judged by fast protein liquid chromatography on Superdex 75 and SDS-polyacrylamide gel electrophoresis. Its optimal pH and optimal temperature were pH 5 and 60 degrees , respectively. The ranking of its activity toward various polyhomoribonucleotides was poly C > poly G > poly A > poly U. It could inhibit proliferation of HepG2 and MCF-7 cancer cells with an IC50 value of 8.6 microM and 7.2 microM, respectively. It was devoid of antifungal and HIV-1 reverse transcriptase inhibitory activity.

Six new oleanane-type triterpenes (1- 6), along with five known compounds, were isolated from the flowers and roots of Saussurea muliensis. On the basis of spectroscopic methods, with special emphasis on 1D and 2D NMR techniques, the structures of the new compounds were characterized as 3beta,22alpha-dihydroxyolean-12-en-30-oic acid (1), 3alpha-(E)-caffeoyloxyolean-12-en-30-oic acid (2), 3alpha-(E)-coumaroyloxyolean-12-en-30-oic acid (3), 3alpha,22alpha-diacetoxy-20beta,21alpha,29-trihydroxy-30-norolean-12-ene (4), 3alpha,22alpha-diacetoxy-21alpha,29-dihydroxy-20beta-methoxy-30-norolean-12-ene (5), and 3alpha,22alpha-diacetoxy-20beta,21alpha-dihydroxy-29-palmityloxy-30-norolean-12-ene (6). The isolated compounds (1- 6) were not active against Staphylococcus aureus, Escherichia coli, Bacillus cereus, and Candida albicans.

The new pyrrolizidine alkaloid glycoside 1, and the three new highly oxygenated bisabolane sesquiterpenes 4–6, together with the two known pyrrolizidine alkaloids 2 and 3, were isolated from the roots of Ligularia cymbulifera (W. W. Smith) Hand.-Mazz. Their structures were established on the basis of spectroscopic analysis, especially 1D- and 2D-NMR data. The cytotoxic activities of compounds 1, 2, and 4–6 were evaluated against hepatoma (BEL-7402), human leukemia (HL-60), human ovarian carcinoma (HO-8910), and nasopharyngeal carcinoma (KB) cell lines (Tables 1–3). Compound 6 showed weak cell-growth inhibition of BEL-7402 cell.

A melibiose- and xylose-cospecific homodimeric lectin was isolated from fresh fruiting bodies of Boletus edulis. The lectin was isolated using a protocol that consisted of ion exchange chromatography on DEAE-cellulose, affinity chromatography on CM-cellulose and gel filtration by fast protein liquid chromatography on Superdex 75. It was a dimer made up of two 16.3 kDa subunits. The hemagglutinating activity of the lectin was stable up to 40 °C, and in the presence of NaOH or HCl solutions up to a concentration of 25 mM. The hemagglutinating activity of the lectin was unaffected in the presence of AlCl3 and FeCl3 at and above 2 mM. MgCl2, ZnCl2 and MnCl2 inhibited the lectin activity. The lectin stimulated the mitogenic response of mouse splenocytes attaining a maximum at 1 μM, and inhibited human immunodeficiency virus-1 reverse transcriptase with an IC50 of 14.3 μM. It did not exhibit antifungal activity.

A novel psychrophilic, yellow-pigmented and obligate aerobic bacterium, strain 0499T, was isolated from the China No.1 glacier. Strain 0499Tdisplayed the common phenotypic and chemotaxonomic features of the genusFlavobacterium, containing menaquinone-6 (MK-6) as the major quinone and C15 : 0, iso-C15 : 0, C17 : 1ω6cand summed feature 3 (C16 : 1ω7c/iso-C15 : 02-OH) as the major fatty acids. Optimal growth occurred at 21 °C. The genomic DNA G+C content was 36.5 mol%. Phylogenetic analysis based on 16S rRNA gene sequence similarity showed that strain 0499Twas related to members of the genusFlavobacterium, sharing the highest sequence similarities withFlavobacterium succinicans(97.9 %),Flavobacterium granuli(97.4 %) andFlavobacterium hydatis(97.2 %). On the basis of phenotypic characteristics, phylogenetic analysis and DNA–DNA relatedness data, a novel speciesFlavobacterium glacieiis proposed with strain 0499T(=CGMCC 1.5380T=JCM 13953T) as the type strain.

A lectin, with a molecular mass of 79 kDa, and with specificity toward rhamnose and O -nitrophenyl-β- d -galactopyranoside, was isolated from samta tomato fruits. The procedure entailed ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on CM-cellulose and gel filtration by fast protein liquid chromatography on Superdex 75. The lectin was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and CM-cellulose. The lectin was stable up to 70 °C. The lectin activity was potentiated by NaOH solutions (25–100 mM), but was reduced by 50 and 100 mM HCl solutions. The activity of the lectin was reduced in the presence of CaCl 2 , MgCl 2 and ZnCl 2 , but was potentiated by 5 and 10 mM AlCl 3 solutions. The lectin stimulated the mitogenic response in mouse splenocytes and inhibited human immunodeficiency virus-1 reverse transcriptase with an IC 50 of 6.2 μM.

A 15 kDa ribonuclease (RNase) was purified from dried fruiting bodies of the wild edible mushroom Armillaria luteo-virens. The simple 4-step purification protocol involved ion-exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion-exchange chromatography on SP-Sepharose and a final gel filtration by FPLC on Superdex-75. The RNase was unadsorbed on Affi-gel blue gel, but adsorbed on DEAE-cellulose and SP-Sepharose. The N-terminal amino acid sequence of purified RNase was AGVQYKLTILLV, which showed low sequence homology to those of previously reported RNases. The optimal pH and temperature of the enzyme were very close to 4.0 and 70 degrees C, respectively. The enzyme showed considerably high ribonucleolytic activity and broad specificity towards polyhomoribonucleotides, with a specificity of poly(U)poly(C)poly (G)poly(A). The ribonucleolytic activities towards poly(U), poly(C), poly(G) and poly(A) were 279.5, 184.1, 69.9 and 52.3 U/mg, respectively.

A monomeric phytase with a molecular mass of 14 kDa was acquired from fresh fruiting bodies of the shiitake mushroomLentinus edodes. The isolation procedure involved chromatography on DEAE-cellulose, CM-cellulose, Q-Sepharose, Affi-gel blue gel, and a final fast protein liquid chromatography-gel filtration on Superdex 75. The purified phytase demonstrated the unique N-terminal amino acid sequence DPKRTDQVN, which exhibited no sequence similarity with those of other phytases previously reported. It expressed its maximal activity at pH 5.0 and 37°C. Phytase activity manifested less than 20% change in activity over the pH range of 3.0–9.0, considerable thermostability with more than 60% residual activity at 70°C, and about 40% residual activity at 95°C. It displayed a wide substrate specificity on a variety of phosphorylated compounds with the following ranking: ATP > fructose-6-phosphate > AMP > glucose-6-phosphate > ADP > sodium phytate >β-glycerophosphate. The phytase activity was moderately stimulated by Ca2+, but inhibited by Al3+, Mn2+, Zn2+, and Cu2+at a tested concentration of 5 mM.

A 36-kDa protein, with an N-terminal sequence highly homologous to polygalacturonase (PG) inhibiting proteins, was isolated from small brown-eyed cowpea seeds. The protein was unadsorbed on diethylaminoethyl cellulose but adsorbed on both Affi-gel blue gel and SP-sepharose. It inhibited mycelial growth in the fungus Mycosphaerella arachidicola with an half-maximal (50%) inhibitory concentration (IC50 ) of 3.3 µM. It reduced [methyl-(3) H] thymidine incorporation into MBL2 lymphoma and L1210 leukemia cells with an IC50 of 7.4 and 5.4 µM, respectively. It inhibited human immunodeficiency virus type 1 (HIV-1) reverse transcriptase with an IC50 of 12.9 µM. However, it did not inhibit PG. The potent antifungal and antitumor activities of the protein suggest that it can be developed into an antifungal agent for combating M. arachidicola invasion in crops and an agent for cancer therapy in humans.

A novel laccase with a molecular mass of 64 kDa and the N-terminal sequence AIGPDDTINF was isolated from fresh fruiting bodies of the mushroom Pleurotus nebrodensis. The purification protocol comprised ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-Sepharose, and gel filtration on Superdex 75. The laccase was adsorbed on DEAE-cellulose and Q-Sepharose, but not on CM-cellulose. It demonstrated an optimal temperature of 70°C. The enzyme activity increased steadily over the temperature range 20°C-70°C. There was only a slight reduction in activity at 80°C. However, all activity disappeared following exposure to 100°C for 10 minutes. The enzyme activity changed only slightly over the pH range 3-5, with the optimum at pH 5, but underwent a precipitous decline when the pH was elevated to 6, and was undetectable at pH 8 and pH 9.

A monomeric acid phosphatase (ACP) with a molecular mass of 72.5 kDa was purified from fresh fruiting bodies of cultured Schizophyllum commune mushroom. The isolation procedure entailed ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. It demonstrated a unique N-terminal amino acid sequence of NAPWAQIDEV, which exhibited 60% amino acid identity to that of S. commune hypothetical histidine ACP based on its genome sequence, but less than 30% amino acid identity to that of other fungal ACPs previously reported. The ACP exhibited an optimum temperature at 50 °C, an optimum pH at pH 4.6, and was considerably stable at a pH range of 4.0 to 9.0, and a temperature range of 20-40 °C. The Km of the purified enzyme for ρ-nitrophenyl phosphate (ρNPP) was 0.248 mM and the Vmax was 9.093 × 10(-3) μM/min. ACP activity was strongly inhibited by Al(3+) and Fe(3+) , but enhanced by Co(2+) , Mg(2+) , and Ca(2+) at a concentration of 0.5 mM.

A monomeric hemolysin with a molecular mass of 29 kDa was isolated from fresh fruiting bodies of the split gill mushroom Schizophyllum commune. The hemolysin was purified by successive adsorption on DEAE-cellulose, carboxymethyl-cellulose and Q-Sepharose and finally gel filtration on Superdex 75. This demonstrated the N-terminal sequence ATNYNKCPGA, different from those of previously reported fungal and bacterial hemolysins. The hemolysin was stable up to 40 degrees C. Only partial activity remained at 50 and 60 degrees C. Activity was indiscernible at 70 degrees C. A pH of 6.0 was optimal for activity. The hemolytic activity was most potently inhibited by dithiothreitol, sucrose and raffinose, followed by cellobiose, maltose, rhamnose, inulin, lactose, fructose and inositol. The metal ions Cu(2+), Mg(2+), Zn(2+), Al(3+) and Fe(3+) significantly, and Pb(2+) to a lesser extent, curtailed the activity of the hemolysin. The hemolysin inhibited HIV-1 reverse transcriptase with an IC(50) of 1.8 microM.

Surgery simulation system can provide a safe virtual training environment. Cutting of soft tissue plays a very important role in the system. During the operation, the soft tissue exhibits nonlinear property and topology change of the operated tissue usually causes the failure of the pre-computed quantity. The above reasons make the simulation of the real-time cutting a challenging task. This paper proposes a new cutting method, based on TLED nonlinear finite element algorithm which deals with real time simulation of deformation. The method combines virtual node algorithm and TLED algorithm, pre-computes related quantities on the element level and locally modifies topology of soft tissue after cutting, avoiding re-computation of pre-computed data. Experiments display its ability to simulate cutting of soft tissue with nonlinear property within real time.

A new antifungal peptide designated as pomegranin, with an N-terminal sequence resembling that of rice disease resistance NB-S-LRR-like protein, was isolated from fresh pomegranate peels by ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, and gel filtration by fast protein liquid chromatography on Superdex 75. Pomegranin was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel. It exhibited a molecular mass of 11 kDa in both gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It inhibited mycelial growth in the fungi Botrytis cinerea and Fusarium oxysporum with an IC(50) of 2 microM and 6.1 microM, respectively. It was devoid of hemagglutinating, ribonuclease, deoxyribonuclease and protease inhibitory activities.

Eight sesquiterpenes, including four guaiane-types containing an interesting epoxy unit (1-4), a rare tricyclic carbon skeleton-type (5) and three eudesmane-types (6-8), along with five known compounds, were isolated from rhizomes of Atractylodes lancea. The structures and relative configurations of 1-8 were determined by analysis of spectroscopic data, and the absolute configuration of 8 was assigned by application of the CD technique. Compounds 1, 2 and 4 were evaluated for their cytotoxic effects against P388 and A549 cells, but all were inactive. Possible biosynthetic pathways for sesquiterpenes (1-8) were discussed.

A novel psychrotolerant, Gram-positive, yellow-pigmented, aerobic bacterium, strain 0549T, was isolated from the China No. 1 glacier. The cells of the isolate were catalase-positive, motile, irregular rods. The diamino acid content of the cell-wall peptidoglycan was determined to be 2,4-diaminobutyric acid. Strain 0549T was able to grow at 4–27 °C, with optimum growth occurring at 20–22 °C. The major fatty acids were anteiso-C15 : 0, anteiso-C15 : 1, iso-C16 : 0 and anteiso-C17 : 0. The genomic DNA G+C content was 67 mol%. A phylogenetic analysis based on 16S rRNA gene sequences indicated that strain 0549T belonged to the genus Cryobacterium and exhibited 96.5 % similarity to Cryobacterium psychrophilum JCM 1463T. On the basis of the phenotypic, chemotaxonomic and phylogenetic properties and the DNA–DNA relatedness data, strain 0549T represents a novel species of the genus Cryobacterium, for which the name Cryobacterium psychrotolerans is proposed. The type strain is 0549T (=CGMCC 1.5382T=JCM 13925T).

A novel bacterial strain, designated 170T, was collected from high latitude Arctic locations (77° 30′ N to approximately 81° 12′ N), including the Canadian Basin and Greenland Sea. Phylogenetic analysis based on 16S rRNA gene sequence comparisons showed that strain 170T was related to members of the genus Glaciecola and had the highest 16S rRNA gene sequence similarity to Glaciecola mesophila. Cells were Gram-negative, psychrophilic, motile rods. The temperature range for growth was 4–15 °C, with optimum growth at 12 °C and at approximately pH 6.0–9.0. Strain 170T contained C16 : 1 ω7c, C16 : 0, C12 : 1 3-OH and C18 : 1 ω7c as major fatty acids. The genomic DNA G+C content was 42.9 mol%. On the basis of phenotypic characterization, phylogenetic analysis and DNA–DNA relatedness data, strain 170T is considered to represent a novel species of the genus Glaciecola, for which the name Glaciecola psychrophila is proposed. The type strain is 170T (=CGMCC 1.6130T=JCM 13954T).

A single-chained antifungal protein with a molecular weight of 6.5 kDa and displaying a novel N-terminal sequence was isolated from dried juvenile cicadas which are used in traditional Chinese medicine, by using ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on SP-Sepharose and then gel filtration on a Superdex peptide column. The peptide, designated cicadin, exerted potent antifungal activity with IC50 values at nonomolar concentrations against a variety of fungi including Botrytis cinerea, Mycosphaerella arachidicola, Fusarium oxysporum, Rhizoctonia solani and Coprinus comatus. Cicadin suppressed the activity of HIV-1 reverse transcriptase and stimulated the proliferation of murine splenocytes.