The Ophiopogon polysaccharides hydrolyzing enzyme production and enzymatic properties have been studied.The results showed that the Absidia sp.O84s strain is the best for enzyme production,the inducer of enzyme is Ophiopogon japonicus-leachate,the optimum condition for enzyme production is at 30 ℃ for 6 days in medium containing 20% Ophiopogon japonicus extract,the optimum temperature for enzyme catalysis is at 40 ℃ and pH 5 for 6 h,and the concentration of substrate is 10 mg/mL.The molecular weight of Ophiopogon polysaccharide is 67 000 u,and its hydrolysates is 39 000 u.
Production of the ginsenoside-β-glucosidasebybacteria GS0202 was optimized.The medium composition is proteose peptone 10 g,yeast powder 5 g,NaCl 10 g.3.2 mg/mL total saponins of Panax ginseng and water 1 L and culture temperature is 28 ℃.The opimum temperature for enzyme catalysis is 25 ℃,pH 4 and the concentration of substrate is 3 mg/mL.
In this paper we propose a novel sparse optical flow (SOF)-based line feature tracking method for the camera pose estimation problem. This method is inspired by the point-based SOF algorithm and developed based on an observation that two adjacent images in time-varying image sequences satisfy brightness invariant. Based on this observation, we re-define the goal of line feature tracking: track two endpoints of a line feature instead of the entire line based on gray value matching instead of descriptor matching. To achieve this goal, an efficient two endpoint tracking (TET) method is presented: first, describe a given line feature with its two endpoints; next, track the two endpoints based on SOF to obtain two new tracked endpoints by minimizing a pixel-level grayscale residual function; finally, connect the two tracked endpoints to generate a new line feature. The correspondence is established between the given and the new line feature. Compared with current descriptor-based methods, our TET method needs not to compute descriptors and detect line features repeatedly. Naturally, it has an obvious advantage over computation. Experiments in several public benchmark datasets show our method yields highly competitive accuracy with an obvious advantage over speed.
Point cloud processing methods exploit local point features and global context through aggregation which does not explicity model the internal correlations between local and global features. To address this problem, we propose full point encoding which is applicable to convolution and transformer architectures. Specifically, we propose Full Point Convolution (FPConv) and Full Point Transformer (FPTransformer) architectures. The key idea is to adaptively learn the weights from local and global geometric connections, where the connections are established through local and global correlation functions respectively. FPConv and FPTransformer simultaneously model the local and global geometric relationships as well as their internal correlations, demonstrating strong generalization ability and high performance. FPConv is incorporated in classical hierarchical network architectures to achieve local and global shape-aware learning. In FPTransformer, we introduce full point position encoding in self-attention, that hierarchically encodes each point position in the global and local receptive field. We also propose a shape aware downsampling block which takes into account the local shape and the global context. Experimental comparison to existing methods on benchmark datasets show the efficacy of FPConv and FPTransformer for semantic segmentation, object detection, classification, and normal estimation tasks. In particular, we achieve state-of-the-art semantic segmentation results of 76% mIoU on S3DIS 6-fold and 72.2% on S3DIS Area5.
The constituent of the medium was investigated for the transformation of tanshinone using Absida sp.T48s.The result showed that the maximum enzyme was produced after incubation of Absida sp.T48s in the soybean cake(65%) medium is for 7 days.The optimum condition for the enzymatic conversion was 45 ℃,pH 5.0;substrate concentration,17.5% and reaction time,13h.
A new beta-glucosidase from a novel strain of Terrabacter ginsenosidimutans (Gsoil 3082(T)) obtained from the soil of a ginseng farm was characterized, and the gene, bgpA (1,947 bp), was cloned in Escherichia coli. The enzyme catalyzed the conversion of ginsenoside Rb1 {3-O-[beta-D-glucopyranosyl-(1-2)-beta-D-glucopyranosyl]-20-O-[beta-D-glucopyranosyl-(1-6)-beta-D-glucopyranosyl]-20(S)-protopanaxadiol} to the more pharmacologically active rare ginsenosides gypenoside XVII {3-O-beta-D-glucopyranosyl-20-O-[beta-D-glucopyranosyl-(1-6)-beta-D-glucopyranosyl]-20(S)-protopanaxadiol}, gypenoside LXXV {20-O-[beta-v-glucopyranosyl-(1-6)-beta-D-glucopyranosyl]-20(S)-protopanaxadiol}, and C-K [20-O-(beta-D-glucopyranosyl)-20(S)-protopanaxadiol]. A BLAST search of the bgpA sequence revealed significant homology to family 3 glycoside hydrolases. Expressed in E. coli, beta-glucosidase had apparent K(m) values of 4.2 +/- 0.8 and 0.14 +/- 0.05 mM and V(max) values of 100.6 +/- 17.1 and 329 +/- 31 micromol x min(-1) x mg of protein(-1) against p-nitrophenyl-beta-D-glucopyranoside and Rb1, respectively. The enzyme catalyzed the hydrolysis of the two glucose moieties attached to the C-3 position of ginsenoside Rb1, and the outer glucose attached to the C-20 position at pH 7.0 and 37 degrees C. These cleavages occurred in a defined order, with the outer glucose of C-3 cleaved first, followed by the inner glucose of C-3, and finally the outer glucose of C-20. These results indicated that BgpA selectively and sequentially converts ginsenoside Rb1 to the rare ginsenosides gypenoside XVII, gypenoside LXXV, and then C-K. Herein is the first report of the cloning and characterization of a novel ginsenoside-transforming beta-glucosidase of the glycoside hydrolase family 3.
[Objective]To sub-clone and express glycosidase gene of Dioscorea nipponica.[Method]The glycosidase gene of Dioscorea nipponica was sub-cloned into Pichia pastoris GS115 expression vector pPIC9K,and the constructed expression vector was transformed into Pichia pastoris GS115 by electroporation method to induce the glycosidase gene.[Result]After have been cultivated for 144 hours in 0.5% methanol,the glycosidase gene in recombinant was proved to be active,and the relative molecular weight of which was 58 kDu through SDS-PAGE analysis.[Conclusion]Glycosidase gene of Dioscorea nipponica was expressed successfully.
'/%3e%3cuse xlink:href='%23a' transform='rotate(23.036 .093 25.536)'/%3e%3cuse xlink:href='%23a' transform='rotate(45.87 1.273 16.18)'/%3e%3cuse xlink:href='%23a' transform='rotate(69.945 .996 12.078)'/%3e%3cuse xlink:href='%23a' transform='rotate(20.66 -19.689 31.932)'/%3e%3c/svg%3e)
'%3e%3cg id='b'%3e%3cpath id='a' stroke='%23000' stroke-width='2' d='M-6-25H6m-12 3H6m-12 3H6'/%3e%3cuse xlink:href='%23a' y='44'/%3e%3c/g%3e%3cpath stroke='%23fff' d='M0 17v10'/%3e%3ccircle r='12' fill='%23cd2e3a'/%3e%3cpath fill='%230047a0' d='M0-12A6 6 0 0 0 0 0a6 6 0 0 1 0 12 12 12 0 0 1 0-24z'/%3e%3c/g%3e%3cg transform='rotate(-123.69)'%3e%3cuse xlink:href='%23b'/%3e%3cpath stroke='%23fff' d='M0-23.5v3M0 17v3.5m0 3v3'/%3e%3c/g%3e%3c/svg%3e)