Search

Strain YJY-8, a new γ-polyglutamic acid producer, was separated from fermented soybean paste samples. The strain was identified as a genus of Bacillus by morphological and 16S rDNA sequence analysis and was named Bacillus sp. YJY-8. The optimal medium composition and cultural conditions were studied using a single-factor experiment and a response surface experiment. The optimized medium consisted of monosodium glutamate 70 g/L, glucose 54.3 g/L, glycerol 31.8 g/L, ammonium sulfate 11.1 g/L, yeast extract 3.2 g/L, tryptone 1.5 g/L, L-glutamic acid 6.8 g/L, MgSO 4 7H 2 O 0.5 g/L, FeCl 3 6H 2 O 0.02 g/L, KH 2 PO 4 0.9 g/L, CaCl 2 0.03 g/L, MnSO 4 H 2 O 0.3 g/L, ammonium molybdate 0.02 g/L, pH 7.0. The optimal cultivation conditions were 35 °C and pH 7.0. Under the optimized conditions, after 48 hr of cultivation, the highest shaking flask fermentation level of γ-PGA reached 65.2 ± 0.36 g/L. In addition, through fed-batch fermentation in 30 L fermenters, the fermentation level of γ-PGA reached its highest level at 88.42 g/L and productivity was 1.23 g/(L hr) after 72 hr. Then, the effect of γ-PGA on tomato yield was investigated. At the seedling stage, the plant height and stem diameter of γ-PGA treated plants increased by 5.69 and 15.735% after spraying γ-PGA for 19 days. During the flowering and fruiting period, the stem diameter of the γ-PGA treatment group increased by 6.74%, with a maximum increase of 11.65%. The number of fruit branches increased by 0.56-16.29% and the number of fruit sets increased by 1.01-28.47%. At the fruit maturation stage, the yield of tomatoes increased by 10.51, 14.27, and 5.83%.

In this study, a high protease-producing strain was screened by spread plate method and identified by molecular biology and morphological identification. It was identified as Bacillus sp. LCB14. A neutral protease gene was cloned and heterologous expressed by B. subtilis SCK6. Then, the recombinant protease was used to dehair the goat skins. The fermentation conditions of neutral protease production by B. subtilis SCK6 were optimized. The single factor experiments, Plackett-Burma experiment, and response surface method were conducted to determine fermentation medium and culture conditions. The optimized medium contained corn meal 49 g/L, soluble starch 28 g/L, soybean meal 17 g/L, corn steep liquor powder 8 g/L, yeast extract 10 g/L, Na 2 HPO 4 2.3 g/L, KH 2 PO 4 1.9 g/L, MgSO 4 0.5 g/L, MnCl 2 0.1 g/L and ZnSO 4 0.05 g/L. The optimized culture conditions were 35 °C and pH 7.0. Under the optimum conditions, the recombinant strain reached 33467.28 U/mL after 72 hr ferment. Moreover, by fed batch in 30 L fermenters, neutral protease production reached 39,440.78 U/mL and shortened fermentation time from 72 hr to 46 hr. Finally, the crude enzyme was utilized to replace sodium sulfide for dehairing of goatskins. The enzymatic dehaired pelts were white, smooth, and soft; the grain side of enzymatic dehaired pelts were clear; there was no obvious damage to the grain side of enzymatic dehaired pelts by visual observation and tactile test. Furthermore, there were no hair roots, hair follicles and other glands in enzymatic dehaired belts, and the collagen fibers of enzymatic dehaired belt were dispersed well by histological analysis.

Resveratrol (1) undergoes microbial transformation when fermented with Streptomyces sp. A12 to yield 3, 5, 4'-trimethoxy-trans-stilbene (2). The structure of the compound 2 was elucidated using the modern spectroscopic techniques. This is the first report of the microbial transformation of resveratrol to compound 2 using the endophyte isolated from Polygonum cuspidatum.

We isolated a moderately halophilic lipase-producing bacterium from the saline soil. Based on the morphological, physiological, chemotaxonomic and phylogenetic analysis, the isolate PT-11 was postulated to be a novel species identified as Oceanobacillus rekensis PT-11. The lipase was purified 2.50-fold by Q-Sepharose FF and SP-Sepharose FF chromatography and its molecular mass was estimated to be 23.5 kDa by SDS-PAGE. It was highly active over the broad temperature ranging from 10 to 35°C and showed up to 80% of the maximum activity at 10°C indicating the lipase to be a typical cold-adapted enzyme. The enzyme activity was slightly enhanced by Na+, Li+ and K+. Incubation with detergents, such as Tween-20 and Tween-80, slightly inhibited the enzyme activity; while Triton X-100decreased the enzyme activity. The enzyme was fairly stable in the presence of long-chain alcohols but was highly denatured in hydrophilic solvents such as acetone or short-chain alcohols (C1-C3).