[1] |
REN B, MIN F F, LIU L Y, et al. Adsorption of different PAM structural units on kaolinite (0 0 1) surface: Density functional theory study [J]. Applied Surface Science, 2020, 504: 144324. doi: 10.1016/j.apsusc.2019.144324
|
[2] |
包木太, 彭杰, 陈庆国. 微生物对聚丙烯酰胺降解作用的研究进展 [J]. 化工进展, 2011, 30(9): 2080-2086. doi: 10.16085/j.issn.1000-6613.2011.09.039
BAO M T, PENG J, CHEN Q G. Research progress of biodegradation of polyacrylamide by microorganisms [J]. Chemical Industry and Engineering Progress, 2011, 30(9): 2080-2086(in Chinese). doi: 10.16085/j.issn.1000-6613.2011.09.039
|
[3] |
LIN Z, LI P T, HOU D, et al. Aggregation mechanism of particles: Effect of Ca2+ and polyacrylamide on coagulation and flocculation of coal slime water containing illite [J]. Minerals, 2017, 7(2): 30. doi: 10.3390/min7020030
|
[4] |
ZOU W J, ZHAO J L, SUN C B. Adsorption of anionic polyacrylamide onto coal and kaolinite calculated from the extended DLVO theory using the van oss-chaudhury-good theory [J]. Polymers, 2018, 10(2): 113. doi: 10.3390/polym10020113
|
[5] |
CASTRO S, LASKOWSKI J S. Depressing effect of flocculants on molybdenite flotation [J]. Minerals Engineering, 2015, 74: 13-19. doi: 10.1016/j.mineng.2014.12.027
|
[6] |
HU H, LIU J F, LI C Y, et al. Anaerobic biodegradation of partially hydrolyzed polyacrylamide in long-term methanogenic enrichment cultures from production water of oil reservoirs [J]. Biodegradation, 2018, 29(3): 233-243. doi: 10.1007/s10532-018-9825-1
|
[7] |
ZHAO L M, BAO M T, YAN M, et al. Kinetics and thermodynamics of biodegradation of hydrolyzed polyacrylamide under anaerobic and aerobic conditions [J]. Bioresource Technology, 2016, 216: 95-104. doi: 10.1016/j.biortech.2016.05.054
|
[8] |
BAO M T, CHEN Q G, LI Y M, et al. Biodegradation of partially hydrolyzed polyacrylamide by bacteria isolated from production water after polymer flooding in an oil field [J]. Journal of Hazardous Materials, 2010, 184(1/2/3): 105-110.
|
[9] |
WEN Q X, CHEN Z Q, ZHAO Y, et al. Biodegradation of polyacrylamide by bacteria isolated from activated sludge and oil-contaminated soil [J]. Journal of Hazardous Materials, 2010, 175(1/2/3): 955-959.
|
[10] |
SONG T W, LI S S, WA D D, et al. Biodegradation of hydrolyzed polyacrylamide by the combined expanded granular sludge bed reactor-aerobic biofilm reactor biosystem and key microorganisms involved in this bioprocess [J]. Bioresource Technology, 2018, 263: 153-162. doi: 10.1016/j.biortech.2018.04.121
|
[11] |
SANG G L, PI Y R, BAO M T, et al. Biodegradation for hydrolyzed polyacrylamide in the anaerobic baffled reactor combined aeration tank [J]. Ecological Engineering, 2015, 84: 121-127. doi: 10.1016/j.ecoleng.2015.07.028
|
[12] |
NYYSSÖLÄ A, AHLGREN J. Microbial degradation of polyacrylamide and the deamination product polyacrylate [J]. International Biodeterioration & Biodegradation, 2019, 139: 24-33.
|
[13] |
林玉珍, 曾光明, 张娱, 等. 有机农药滴滴涕和毒死蜱生物降解机制的分子模拟研究 [J]. 环境科学, 2012, 33(3): 1015-1019.
LIN Y Z, ZENG G M, ZHANG Y, et al. Biodegradation mechanism of DDT and chlorpyrifos using molecular simulation [J]. Environmental Science, 2012, 33(3): 1015-1019(in Chinese).
|
[14] |
LIU Z F, SHAO B B, ZENG G M, et al. Effects of rhamnolipids on the removal of 2, 4, 2, 4-tetrabrominated biphenyl ether (BDE-47) by Phanerochaete chrysosporium analyzed with a combined approach of experiments and molecular docking [J]. Chemosphere, 2018, 210: 922-930. doi: 10.1016/j.chemosphere.2018.07.114
|
[15] |
ZHANG Y, ZENG Z T, ZENG G M, et al. Enzyme-substrate binding landscapes in the process of nitrile biodegradation mediated by nitrile hydratase and amidase [J]. Applied Biochemistry and Biotechnology, 2013, 170(7): 1614-1623. doi: 10.1007/s12010-013-0276-1
|
[16] |
ZHAO L M, ZHANG C C, LU Z Y, et al. Key role of different levels of dissolved oxygen in hydrolyzed polyacrylamide bioconversion: Focusing on metabolic products, key enzymes and functional microorganisms [J]. Bioresource Technology, 2020, 306: 123089. doi: 10.1016/j.biortech.2020.123089
|
[17] |
KAY-SHOEMAKE J L, WATWOOD M E, LENTZ R D, et al. Polyacrylamide as an organic nitrogen source for soil microorganisms with potential effects on inorganic soil nitrogen in agricultural soil [J]. Soil Biology and Biochemistry, 1998, 30(8/9): 1045-1052.
|
[18] |
KAY-SHOEMAKE J L, WATWOOD M E, SOJKA R E, et al. Polyacrylamide as a substrate for microbial amidase in culture and soil [J]. Soil Biology and Biochemistry, 1998, 30(13): 1647-1654. doi: 10.1016/S0038-0717(97)00251-4
|
[19] |
OHTAKI A, MURATA K, SATO Y, et al. Structure and characterization of amidase from Rhodococcus sp. N-771: Insight into the molecular mechanism of substrate recognition [J]. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2010, 1804(1): 184-192. doi: 10.1016/j.bbapap.2009.10.001
|
[20] |
ZHAO X D, SONG L Z, FU J, et al. Experimental and DFT investigation of surface degradation of polyvinylidene fluoride membrane in alkaline solution [J]. Surface Science, 2011, 605(11/12): 1005-1015.
|
[21] |
TU M L, WANG C, CHEN C, et al. Identification of a novel ACE-inhibitory peptide from casein and evaluation of the inhibitory mechanisms [J]. Food Chemistry, 2018, 256: 98-104. doi: 10.1016/j.foodchem.2018.02.107
|
[22] |
CHEN M, ZENG G M, LAI C, et al. Molecular basis of laccase bound to lignin: Insight from comparative studies on the interaction of Trametes versicolor laccase with various lignin model compounds [J]. RSC Advances, 2015, 5(65): 52307-52313. doi: 10.1039/C5RA07916K
|
[23] |
刘文强, 黄露义, 李国菠. 采用药效团模型和分子对接方法筛选新型的组蛋白甲基转移酶G9a抑制剂 [J]. 西北药学杂志, 2016, 31(2): 186-189. doi: 10.3969/j.issn.1004-2407.2016.02.022
LIU W Q, HUANG L Y, LI G B. Virtual screening of novel histone methyltransferase G9a inhibitors by using pharmacophore modeling and molecular docking [J]. Northwest Pharmaceutical Journal, 2016, 31(2): 186-189(in Chinese). doi: 10.3969/j.issn.1004-2407.2016.02.022
|
[24] |
TU M L, LIU H X, ZHANG R Y, et al. Analysis and evaluation of the inhibitory mechanism of a novel angiotensin-I-converting enzyme inhibitory peptide derived from casein hydrolysate [J]. Journal of Agricultural and Food Chemistry, 2018, 66(16): 4139-4144. doi: 10.1021/acs.jafc.8b00732
|