2009
DOI: 10.1016/j.molstruc.2009.08.036
|View full text |Cite
|
Sign up to set email alerts
|

Characterisation of keratin biomass from butchery and wool industry wastes

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

2
108
0
3

Year Published

2013
2013
2020
2020

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 149 publications
(113 citation statements)
references
References 30 publications
2
108
0
3
Order By: Relevance
“…After the first 5 h, the release of the drug from K/G and K/C blend films was faster than the other films and gradually increased until reaching 100% after 12 h of study. Surprisingly, the K/S blend film released about 50% of the drug after 12 h and was empty within 49 h. At the end of the experiment, the K/S released drug was about 60%, while the native keratin showed the lowest release of the drug, about 15% at 49 h. The drug release profile of the blend films was studied by immersion in PBS with stirring for 49 h. This was in accordance with the dissolution of keratin, since it is composed of a high content of sulfur from the amino acid cystein 16 . The disulfide (-S-S-) in the keratin structure was a main factor in the dissolution and drug release protection.…”
Section: Drug Release Studymentioning
confidence: 81%
See 2 more Smart Citations
“…After the first 5 h, the release of the drug from K/G and K/C blend films was faster than the other films and gradually increased until reaching 100% after 12 h of study. Surprisingly, the K/S blend film released about 50% of the drug after 12 h and was empty within 49 h. At the end of the experiment, the K/S released drug was about 60%, while the native keratin showed the lowest release of the drug, about 15% at 49 h. The drug release profile of the blend films was studied by immersion in PBS with stirring for 49 h. This was in accordance with the dissolution of keratin, since it is composed of a high content of sulfur from the amino acid cystein 16 . The disulfide (-S-S-) in the keratin structure was a main factor in the dissolution and drug release protection.…”
Section: Drug Release Studymentioning
confidence: 81%
“…The texture of the keratin film was fragile and brittle due to the strong disulfide bond from the cystine molecules 16 . Many polar natural polymers including sericin, collagen peptide, gelatin and starch were chosen for improving the keratin texture.…”
Section: Digital Images Of Keratin Filmsmentioning
confidence: 99%
See 1 more Smart Citation
“…The ratio of sulphur content also play important role in physical properties of keratin. Some researchers classified keratin as soft and hard forms based upon sulphur content (Rizvi and Khan 2008;Zoccola et al 2009). Soft keratin has lower cystine content, week cross linking and smaller resistant to other chemicals found in the hair core and outer layer of epidermis (Fraser et al 1972).…”
Section: Introductionmentioning
confidence: 99%
“…On the bright side, most of these AFs are keratinous materials; that is, they are potential bio-resources for keratin extraction [26] [27].…”
Section: Introductionmentioning
confidence: 99%