Institution
Zhejiang Gongshang University
Education•Hangzhou, China•
About: Zhejiang Gongshang University is a education organization based out in Hangzhou, China. It is known for research contribution in the topics: Adsorption & Supply chain. The organization has 8258 authors who have published 7670 publications receiving 90296 citations. The organization is also known as: Zhèjiāng Gōngshāng Dàxué.
Topics: Adsorption, Supply chain, Population, Wireless sensor network, Catalysis
Papers published on a yearly basis
Papers
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TL;DR: It was found that E. coli was a suitable host for heterologous expression of plantaricin NC8 with a significant yield and appeared to be very active for controlling and inhibiting the food-borne pathogenic Gram-negative bacteria Salmonella spp.
44 citations
TL;DR: In conclusion, peer-induced fairness concern scenario is the best scenario for the retailer, whereas no fairness concern on either side is preferred for the two manufacturers.
44 citations
TL;DR: In this paper, an experimental design using response surface methodology (RSM) was used to optimize the process parameters in esterification to minimize rigorous experimental procedures and conserve the catalyst.
44 citations
TL;DR: The characterization results demonstrate that the multi-stepped horn configuration has the potential to improve the performance of ultrasound as an advanced oxidation technology by increasing the cavitation zone in the solution.
44 citations
TL;DR: The results suggest that the purified enzyme was a cathepsin L-like enzyme and that it existed in the form of its enzyme-inhibitor complex or precursor.
Abstract: Cathepsin L-like enzyme was purified from the body wall of the sea cucumber Stichopus japonicus by an integral method involving ammonium sulfate precipitation and a series of column chromatographies on DEAE Sepharose CL-6B, Sephadex G-75, and TSK-GEL. The molecular mass of the purified enzyme was estimated to be 63 kDa by SDS-PAGE. The enzyme cleaved N-carbobenzoxy-phenylalanine-arginine7-amido-4-methylcoumarin with K(m) (69.92 microM) and k(cat) (12.80/S) hardly hydrolyzed N-carbobenzoxy-arginine-arginine 7-amido-4-methylcoumarin and L-arginine 7-amido-4-methylcoumarin. The optimum pH and temperature for the purified enzyme were found to be 5.0 and 50 degrees C. It showed thermal stability below 40 degrees C. The activity was inhibited by sulfhydryl reagents and activated by reducing agents. These results suggest that the purified enzyme was a cathepsin L-like enzyme and that it existed in the form of its enzyme-inhibitor complex or precursor.
44 citations
Authors
Showing all 8318 results
| Name | H-index | Papers | Citations |
|---|---|---|---|
| David Julian McClements | 131 | 1137 | 71123 |
| Sajal K. Das | 85 | 1124 | 29785 |
| Ye Wang | 85 | 466 | 24052 |
| Xun Wang | 84 | 606 | 32187 |
| Tao Jiang | 82 | 940 | 27018 |
| Yueming Jiang | 79 | 452 | 20563 |
| Mo Wang | 61 | 274 | 13664 |
| Robert J. Linhardt | 58 | 1190 | 53368 |
| Jiankun Hu | 57 | 493 | 11430 |
| Xuming Zhang | 56 | 384 | 10788 |
| Yuan Li | 50 | 352 | 8771 |
| Chunping Yang | 49 | 173 | 8604 |
| Duo Li | 48 | 329 | 9060 |
| Matthew Campbell | 48 | 236 | 13448 |
| Aiqian Ye | 48 | 163 | 6120 |