|
|
|
|
| LEADER |
01000naa a22002652 4500 |
| 001 |
NLM169579433 |
| 003 |
DE-627 |
| 005 |
20231223121632.0 |
| 007 |
tu |
| 008 |
231223s2007 xx ||||| 00| ||eng c |
| 028 |
5 |
2 |
|a pubmed24n0565.xml
|
| 035 |
|
|
|a (DE-627)NLM169579433
|
| 035 |
|
|
|a (NLM)17425338
|
| 040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rakwb
|
| 041 |
|
|
|a eng
|
| 100 |
1 |
|
|a Rangnekar, Abhijit
|e verfasserin
|4 aut
|
| 245 |
1 |
0 |
|a Retention of enzymatic activity of alpha-amylase in the reductive synthesis of gold nanoparticles
|
| 264 |
|
1 |
|c 2007
|
| 336 |
|
|
|a Text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
|
| 338 |
|
|
|a Band
|b nc
|2 rdacarrier
|
| 500 |
|
|
|a Date Completed 27.06.2007
|
| 500 |
|
|
|a Date Revised 21.11.2008
|
| 500 |
|
|
|a published: Print-Electronic
|
| 500 |
|
|
|a Citation Status MEDLINE
|
| 520 |
|
|
|a In this paper, we report the generation of Au nanoparticles (NPs), using a pure enzyme for the reduction of AuCl4(-), with the retention of enzymatic activity in the complex. As a model system, alpha-amylase was used to readily synthesize and stabilize Au NPs in aqueous solution. Although several other enzymes were also pursued for the synthesis, it was interesting to observe that only alpha-amylase and EcoRI could produce Au NPs. Following NP synthesis, the activity of the enzyme was retained in the Au NP-alpha-amylase complex. The presence of Au NPs and alpha-amylase in the complex was established by UV-visible and FT-IR spectroscopy, X-ray diffraction (XRD) and transmission electron microscopic (TEM) measurements. Our observations suggest that the presence of free and exposed S-H groups is essential in the reduction of AuCl4(-) to Au NPs. Structural analysis of the enzymes showed that both alpha-amylase and EcoRI enzymes have free and exposed S-H groups in their native form and thus are suitable for the generation of NPs, whereas the other ones used here do not have such groups. Fortuitously, the enzymatic functional group of alpha-amylase is positioned opposite to that of the free and exposed S-H group, which makes it ideal for the production of Au NPs; binding of the enzyme to Au NPs via Au-S bond and also retention of the biological activity of the enzyme
|
| 650 |
|
4 |
|a Journal Article
|
| 650 |
|
4 |
|a Research Support, Non-U.S. Gov't
|
| 650 |
|
7 |
|a Chlorides
|2 NLM
|
| 650 |
|
7 |
|a Sulfides
|2 NLM
|
| 650 |
|
7 |
|a Gold
|2 NLM
|
| 650 |
|
7 |
|a 7440-57-5
|2 NLM
|
| 650 |
|
7 |
|a Deoxyribonuclease EcoRI
|2 NLM
|
| 650 |
|
7 |
|a EC 3.1.21.-
|2 NLM
|
| 650 |
|
7 |
|a alpha-Amylases
|2 NLM
|
| 650 |
|
7 |
|a EC 3.2.1.1
|2 NLM
|
| 700 |
1 |
|
|a Sarma, Tridib Kumar
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Singh, Atul Kumar
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Deka, Jashmini
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Ramesh, Aiyagari
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Chattopadhyay, Arun
|e verfasserin
|4 aut
|
| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 23(2007), 10 vom: 08. Mai, Seite 5700-6
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
|
| 773 |
1 |
8 |
|g volume:23
|g year:2007
|g number:10
|g day:08
|g month:05
|g pages:5700-6
|
| 912 |
|
|
|a GBV_USEFLAG_A
|
| 912 |
|
|
|a SYSFLAG_A
|
| 912 |
|
|
|a GBV_NLM
|
| 912 |
|
|
|a GBV_ILN_22
|
| 912 |
|
|
|a GBV_ILN_350
|
| 912 |
|
|
|a GBV_ILN_721
|
| 951 |
|
|
|a AR
|
| 952 |
|
|
|d 23
|j 2007
|e 10
|b 08
|c 05
|h 5700-6
|