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Evaluation of the YOLO models for discrimination of the alfalfa pollinating bee species
Zhang Chuan-Jie,Liu Teng,Wang Jinxu,Zhai Danlan,Zhang Youxin,Gao Yang,Wu Hui-Zhen,Yu Jialin,Chen Min 한국응용곤충학회 2024 Journal of Asia-Pacific Entomology Vol.27 No.1
Identifying insect pollinators and their roles in mediating pollen flow is critical to understand the potential gene flow risks of insect pollination-dependent crop species, such as alfalfa. This study was conducted to evaluate and compare the feasibility of You Only Look Once (YOLO) version 3 (YOLOv3), YOLOv5, YOLOv7, and YOLO Representation (YOLOR) to discriminate the three most common alfalfa pollinating bee species, including honeybee, bumblebee, and leafcutting bee. The metrics comparison results showed YOLOv3 and YOLOv5 out performed YOLOv7 and YOLOR regarding model precision, recall, F 1 score, and mAP50 values. YOLOv3 and YOLOv5 could successfully discriminate the three different bee species with an accuracy of almost 100% (99.9%, 99.8%, and 100% accuracy for honeybee, bumblebee, and leafcutting bee for the two models, respectively). Comparatively, YOLOv7 could discriminate honeybee with an accuracy of 95% but was more likely to mistakenly discriminate bumblebee and leafcutting bee due to the relatively lower discriminating accuracy (87.3% and 66.2%, respectively). While the values of determined parameters for YOLOR were lower than YOLOv3 and YOLOv5, the higher precision (0.99680) along with recall (0.98721), F 1 (0.99198), mAP50 (0.99323), and mAP50-100 (0.89076) values indicate that this model could be able to obtain a favorable performance in discriminating the three bee species. In summary, the proposed method in this study has the potential for identifying the alfalfa pollinating bee species, studying the bees’ flower-visiting behaviors, evaluating the risks of insect-mediated pollen flow, and thus contributing to the management of genetically engineered (GE) alfalfa transgene flow.
( Jin Xu ),( Xuejia Shi ),( Xiaomeng Zhang ),( Zhenzhong Wang ),( Wei Xiao ),( Linguo Zhao ) 한국미생물생명공학회(구 한국산업미생물학회) 2021 Journal of microbiology and biotechnology Vol.31 No.3
To efficiently recycle GH78 thermostable rhamnosidase (TpeRha) and easily separate it from the reaction mixture and furtherly improve the enzyme properties, the magnetic particle Fe<sub>3</sub>O<sub>4</sub>-SiO<sub>2</sub>-NH<sub>2</sub>-Cellu-ZIF8 (FSNcZ8) was prepared by modifying Fe<sub>3</sub>O<sub>4</sub>-NH<sub>2</sub> with tetraethyl silicate (TEOS), microcrystalline cellulose and zinc nitrate hexahydrate. FSNcZ8 displayed better magnetic stability and higher-temperature stability than unmodified Fe<sub>3</sub>O<sub>4</sub>-NH<sub>2</sub> (FN), and it was used to adsorb and immobilize TpeRha from Thermotoga petrophilea 13995. As for properties, FSNcZ8-TpeRha showed optimal reaction temperature and pH of 90℃ and 5.0, while its highest activity approached 714 U/g. In addition, FSNcZ8-TpeRha had better higher-temperature stability than FN. After incubation at 80℃ for 3 h, the residual enzyme activities of FSNcZ8-TpeRha, FN-TpeRha and free enzyme were 93.5%, 63.32%, and 62.77%, respectively. The organic solvent tolerance and the monosaccharides tolerance of FSNcZ8-TpeRha, compared with free TpeRha, were greatly improved. Using naringin (1 mmol/l) as the substrate, the optimal conversion conditions were as follows: FSNcZ8-TpeRha concentration was 6 U/ml; induction temperature was 80℃; the pH was 5.5; induction time was 30 min, and the yield of products was the same as free enzyme. After repeating the reaction 10 times, the conversion of naringin remained above 80%, showing great improvement of the catalytic efficiency and repeated utilization of the immobilized α-L-rhamnosidase.