A novel alginate-degrading marine bacterium Microbulbifer sp. ALW1 was isolated from rotten brown alga. An extracellular alginate lyase was purified to electrophoretic homogeneity and had a molecular mass of about 26.0 kDa determined by SDS-PAGE and size exclusion chromatography. This enzyme showed activities towards both polyguluronate and polymannuronate indicating its bifunctionality while with preference for the former substrate. Using sodium alginate as a substrate, strain ALW1 alginate lyase was optimally active at 45 °C and pH 7.0. It was stable at 25 °C, 30 °C, 35 °C and 40 °C, but not stable at 50 °C. This alginate lyase showed good stability over a broad pH range (5.0-9.0). The enzyme activity was increased to 5.1 times by adding NaCl to a final concentration of 0.5M. Strain ALW1 alginate lyase produced disaccharide (majority) and trisaccharide from alginate indicating that this enzyme could be a good tool for preparation of alginate oligosaccharides with low degree of polymerization (DP). The alginate oligosaccharides displayed the scavenging abilities towards radicals (DPPH, ABTS(+) and hydroxyl) and the reducing power. Therefore, the hydrolysates exhibited the antioxidant activity and had potential as a natural antioxidant.

Abstract-Affective factors are the most important factors in SLA and English teaching. These factors include emotion, feeling, mood, manner, attitude and so on. All these factors, especially, motivation, self-confidence and anxiety, decide the input and output of the second language. Under the guidance of the Affective Filter Hypothesis proposed by Krashen, the present paper makes a survey on advanced English majors. By collecting and analyzing research data, some useful results and implications have been found and can be used in future teaching. The affective factors will surely help the teachers to improve their teaching quality and students to cultivate an all-round development.

Light is a major environmental signal for insect circadian. In this study, we isolated two cryptochrome (cry) genes from Helicoverpa armigera (Hübner) by reverse transcription polymerase chain reaction and RACE-PCR strategies, designated as Ha-cryl (GenBank accession GQ896502) and Ha-cry2 (GenBank accession GQ896503). Ha-CRY1 encoded a fly-like protein of 548 amino acids, while Ha-CRY2 encoded a mammal-like protein of 657 amino acids. Both of these proteins had two conserved domains: a DNA photolyase domain and a flavin adenine dinucleotide (FAD) binding seven domain, and alignment of the amino acid sequence indicated that there was a high degree of homology between the CRYs of H. armigera and other insects. Real-time polymerase chain reaction revealed that: 1) Ha-cry1 and Ha-cry2 mRNA expressions were neither organ-specific nor developmental-stage-specific. 2) Under the light-dark cycle (16:8 L:D), Ha-cry1 abundance tended to increase during the day, then decrease in the night, whereas the expression pattern of Ha-cry2 was opposite. 3) The cyclings of Ha-cry1 and Ha-cry2 expression were disturbed by constant light and darkness. Our study has significant importance for the further study of the functions of the Ha-cry genes and potential control of the cotton bollworm.

A naringinase from Aspergillus aculeatus JMUdb058 was purified, identified, and characterized. This naringinase had a molecular mass (MW) of 348 kDa and contained four subunits with MWs of 100, 95, 84, and 69 kDa. Mass spectrometric analysis revealed that the three larger subunits were β-D-glucosidases and that the smallest subunit was an α-L-rhamnosidase. The naringinase and its α-L-rhamnosidase and β-D-glucosidase subunits all had optimal activities at approximately pH 4 and 50 °C, and they were stable between pH 3 and 6 and below 50 °C. This naringinase was able to hydrolyze naringin, aesculin, and some other glycosides. The enzyme complex had a K(m) value of 0.11 mM and a k(cat)/K(m) ratio of 14,034 s(-1) mM(-1) for total naringinase. Its α-L-rhamnosidase and β-D-glucosidase subunits had K(m) values of 0.23 and 0.53 mM, respectively, and k(cat)/K(m) ratios of 14,146 and 7733 s(-1) mM(-1), respectively. These results provide in-depth insight into the structure of the naringinase complex and the hydrolyses of naringin and other glycosides.

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