Molecular docking analysis of subtilisin-like alkaline serine protease (SLASP) and laccase with natural biopolymers
Alkaline serine proteases (ASPs) and laccases (Lacs) have been reported to possess several industrial applications, particularly in the food, cosmetic, and leather industries. Thus, in the present study, eighteen natural biopolymers, including agar, agarose, alginate, kappa carrageenan, cellulose, c...
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| Published in | Open Chemistry Vol. 22; no. 1; pp. 69 - 78 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
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De Gruyter
30.09.2024
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| Subjects | |
| Online Access | Get full text |
| ISSN | 2391-5420 2391-5420 |
| DOI | 10.1515/chem-2024-0090 |
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| Abstract | Alkaline serine proteases (ASPs) and laccases (Lacs) have been reported to possess several industrial applications, particularly in the food, cosmetic, and leather industries. Thus, in the present study, eighteen natural biopolymers, including agar, agarose, alginate, kappa carrageenan, cellulose, chitosan pentamer, chitosan oligosaccharide, chondroitin sulfate, dextran, fucoidan, heparin, hyaluronan, lignin, mannan, pectin, phytic acid, pullulan and starch soluble, were studied for their docking behavior, such as subtilisin-like alkaline serine protease (SLASP) KP-43 and
laccase (Bs Lac), using the SwissDock method. Additionally, the toxicity toward honey bees and human liver was determined by utilizing the free Bee-Tox and pkCSM web servers, respectively. Bee-Tox analysis demonstrated that four ligands (namely, agar, cellulose, lignin, and pullulan) exhibited acute oral toxicity toward honey bees (
). The docking study revealed that chitosan pentamer and lignin exhibited maximum binding energies of −9.67 and −11.37 kcal/mol against the target proteins SLASP (KP-43) and Lac (Bs Lac), respectively. Interestingly, in the present study, agarose was shown to interact with the His68 and Ser255 amino acid residues of SLASP (KP-43) from KSM-KP43
sp. Thus, the current investigation showed the potential of eighteen natural biopolymers as immobilizing agents to prepare ASP and Lac nanoparticles for biomedical applications. |
|---|---|
| AbstractList | Alkaline serine proteases (ASPs) and laccases (Lacs) have been reported to possess several industrial applications, particularly in the food, cosmetic, and leather industries. Thus, in the present study, eighteen natural biopolymers, including agar, agarose, alginate, kappa carrageenan, cellulose, chitosan pentamer, chitosan oligosaccharide, chondroitin sulfate, dextran, fucoidan, heparin, hyaluronan, lignin, mannan, pectin, phytic acid, pullulan and starch soluble, were studied for their docking behavior, such as subtilisin-like alkaline serine protease (SLASP) KP-43 and
laccase (Bs Lac), using the SwissDock method. Additionally, the toxicity toward honey bees and human liver was determined by utilizing the free Bee-Tox and pkCSM web servers, respectively. Bee-Tox analysis demonstrated that four ligands (namely, agar, cellulose, lignin, and pullulan) exhibited acute oral toxicity toward honey bees (
). The docking study revealed that chitosan pentamer and lignin exhibited maximum binding energies of −9.67 and −11.37 kcal/mol against the target proteins SLASP (KP-43) and Lac (Bs Lac), respectively. Interestingly, in the present study, agarose was shown to interact with the His68 and Ser255 amino acid residues of SLASP (KP-43) from KSM-KP43
sp. Thus, the current investigation showed the potential of eighteen natural biopolymers as immobilizing agents to prepare ASP and Lac nanoparticles for biomedical applications. Alkaline serine proteases (ASPs) and laccases (Lacs) have been reported to possess several industrial applications, particularly in the food, cosmetic, and leather industries. Thus, in the present study, eighteen natural biopolymers, including agar, agarose, alginate, kappa carrageenan, cellulose, chitosan pentamer, chitosan oligosaccharide, chondroitin sulfate, dextran, fucoidan, heparin, hyaluronan, lignin, mannan, pectin, phytic acid, pullulan and starch soluble, were studied for their docking behavior, such as subtilisin-like alkaline serine protease (SLASP) KP-43 and Bacillus subtilis laccase (Bs Lac), using the SwissDock method. Additionally, the toxicity toward honey bees and human liver was determined by utilizing the free Bee-Tox and pkCSM web servers, respectively. Bee-Tox analysis demonstrated that four ligands (namely, agar, cellulose, lignin, and pullulan) exhibited acute oral toxicity toward honey bees ( Apis mellifera ). The docking study revealed that chitosan pentamer and lignin exhibited maximum binding energies of −9.67 and −11.37 kcal/mol against the target proteins SLASP (KP-43) and Lac (Bs Lac), respectively. Interestingly, in the present study, agarose was shown to interact with the His68 and Ser255 amino acid residues of SLASP (KP-43) from KSM-KP43 Bacillus sp. Thus, the current investigation showed the potential of eighteen natural biopolymers as immobilizing agents to prepare ASP and Lac nanoparticles for biomedical applications. |
| Author | Prabhakaran, Vasantha-Srinivasan Al-Otibi, Fatimah Oleyan Narayanaswamy, Radhakrishnan Ibrahim, Kalibulla Syed Alharbi, Raedah Ibrahim |
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| Cites_doi | 10.1016/j.neuron.2018.08.011 10.1039/D1NJ02938J 10.1155/2012/823830 10.1016/j.sjbs.2024.104009 10.1080/08905436.2011.617258 10.3390/catal10060697 10.3389/fmicb.2016.01195 10.1007/s00894-009-0454-9 10.1016/j.carbpol.2012.10.045 10.1002/app.49669 10.3390/catal11101211 10.1016/j.biortech.2011.09.076 10.4137/BBI.S40427 10.3390/toxics11080660 10.29252/JABR.05.03.01 10.1074/jbc.M409089200 10.1002/pro.5560060301 10.1016/B978-0-323-41736-5.00004-2 10.31788/RJC.2020.1315541 10.1016/j.jclepro.2022.134296 10.1016/j.jclepro.2021.130243 10.33263/BRIAC111.78477859 10.4061/2011/217861 10.1016/j.ijbiomac.2021.10.020 10.3389/fbioe.2020.00222 10.1039/b800584b 10.1093/bioinformatics/btt055 10.1016/S1001-0742(08)62559-0 10.1016/j.bcab.2017.11.016 10.1080/17435390.2020.1842537 10.1093/nar/gkr366 10.1093/nar/gkx312 10.2174/1566524021666211018113204 10.1371/journal.pone.0116524 10.1016/j.ailsci.2021.100013 10.1002/jobm.201500341 10.3390/pr8010016 10.1089/ind.2018.0032 10.1007/s00253-020-10826-2 10.1016/j.molliq.2022.118901 10.1016/j.heliyon.2021.e08148 10.1016/j.bpj.2017.03.011 10.1016/j.reactfunctpolym.2021.105005 10.1016/j.jsb.2015.03.005 10.1016/j.ijbiomac.2015.08.011 |
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| SubjectTerms | bacillus subtilis laccase chitosan laccase MD simulation molecular docking nanoparticles natural biopolymer subtilisin-like alkaline serine protease |
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| Title | Molecular docking analysis of subtilisin-like alkaline serine protease (SLASP) and laccase with natural biopolymers |
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