Investigating the Effect of Under-Zero Treatment (−80 and −196 °C) to Silk Protein

2017 ◽  
pp. 667-670
Author(s):  
Anh-Hien Tran ◽  
Thu-Hien Luong ◽  
Xuan-Thanh Le ◽  
Thi-Hiep Nguyen ◽  
Toi Vo Van
Keyword(s):  
Silk Protein

scholarly journals Changes in Amino Acid Profiles and Bioactive Compounds of Thai Silk Cocoons as Affected by Water Extraction

Molecules ◽  
2021 ◽  
Vol 26 (7) ◽  
pp. 2033
Author(s):  
Chuleeporn Bungthong ◽  
Sirithon Siriamornpun
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Biological Activities ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Silk Protein ◽  
Extraction Time ◽  
Antioxidant Power ◽  
Silk Cocoon ◽  
Amino Acid Profiles

Silk proteins have many advantageous components including proteins and pigments. The proteins—sericin and fibroin—have been widely studied for medical applications due to their good physiochemical properties and biological activities. Various strains of cocoon display different compositions such as amino-acid profiles and levels of antioxidant activity. Therefore, the objectives of this study were to find a suitable silk protein extraction method to obtain products with chemical and biological properties suitable as functional foods in two strains of Bombyx mori silk cocoon (Nangsew strains; yellow cocoon) and Samia ricini silk cocoon (Eri strains; white cocoon) extracted by water at 100 °C for 2, 4, 6 and 8 h. The results showed that Nangsew strains extracted for 6 h contained the highest amounts of protein, amino acids, total phenolics (TPC) and total flavonoids (TFC), plus DPPH radical-scavenging activity, ABTS radical scavenging capacity, and ferric reducing antioxidant power (FRAP), anti-glycation, α-amylase and α-glucosidase inhibition. The longer extraction time produced higher concentrations of amino acids, contributing to sweet and umami tastes in both silk strains. It seemed that the bitterness decreased as the extraction time increased, resulting in improvements in the sweetness and umami of silk-protein extracts.

scholarly journals Functional silk fibroin hydrogels: preparation, properties and applications

2021 ◽  
Author(s):  
Haiyan Zheng ◽  
Baoqi Zuo
Keyword(s):  
Silk Fibroin ◽  
Silk Protein ◽  
Current Status ◽  
Protein Hydrogels

This article reviews the current status of the preparation, properties and application of functional silk protein hydrogels.

Studying on Preperation and Emulsifying Properties of Silk Protein Calcium Salt Made from Waste Silk

2011 ◽  
Vol 197-198 ◽  
pp. 60-64 ◽  
Author(s):  
Jun Sheng Li ◽  
Hai Tao Cheng
Keyword(s):  
Aqueous Solution ◽  
Calcium Chloride ◽  
Salt Solution ◽  
Chloride Solution ◽  
Calcium Salt ◽  
Calcium Chloride Solution ◽  
Silk Protein ◽  
Emulsifying Properties ◽  
Emulsification Capacity ◽  
New Protein

One key step for silk protein further uses is to let them be dissolved in aqueous solution. However, the silk protein is usually not soluble in aqueous solution. Silk protein dissolved in calcium chloride solution is one of the few effective ways. Silk fibroin was well dissolved in 15-20min. in boiling calcium chloride solution [50% (w/v)] with the ratio of 15g dry waste silk per100mL calcium chloride solution. After dialysis, silk protein calcium salt unexpectedly showed excellent emulsification capacity and stability. Only 0.8-1.2% of silk protein calcium salt solution (50mL) could let 50mL soybean salad oil be mixed and emulsified well. Silk protein calcium salt may be used as a new protein-based surfactant.

The fractal self-assembly of the silk protein sericin

Soft Matter ◽  
2010 ◽  
Vol 6 (9) ◽  
pp. 2066 ◽  
Author(s):  
Tejas S. Khire ◽  
Joydip Kundu ◽  
Subhas C. Kundu ◽  
Vamsi K. Yadavalli
Keyword(s):  
Self Assembly ◽  
Silk Protein

scholarly journals Presence of β-Turn Structure in Recombinant Spider Silk Dissolved in Formic Acid Revealed with NMR

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 511
Author(s):  
Yu Suzuki ◽  
Takanori Higashi ◽  
Takahiro Yamamoto ◽  
Hideyasu Okamura ◽  
Takehiro K. Sato ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Formic Acid ◽  
Spider Silk ◽  
Chemical Shifts ◽  
Repetitive Sequences ◽  
Silk Protein ◽  
Random Coil ◽  
Oh Groups ◽  
Spider Silk Protein ◽  
Turn Structure

Spider dragline silk is a biopolymer with excellent mechanical properties. The development of recombinant spider silk protein (RSP)-based materials with these properties is desirable. Formic acid (FA) is a spinning solvent for regenerated Bombyx mori silk fiber with excellent mechanical properties. To use FA as a spinning solvent for RSP with the sequence of major ampullate spider silk protein from Araneus diadematus, we determined the conformation of RSP in FA using solution NMR to determine the role of FA as a spinning solvent. We assigned 1H, 13C, and 15N chemical shifts to 32-residue repetitive sequences, including polyAla and Gly-rich regions of RSP. Chemical shift evaluation revealed that RSP is in mainly random coil conformation with partially type II β-turn structure in the Gly-Pro-Gly-X motifs of the Gly-rich region in FA, which was confirmed by the 15N NOE data. In addition, formylation at the Ser OH groups occurred in FA. Furthermore, we evaluated the conformation of the as-cast film of RSP dissolved in FA using solid-state NMR and found that β-sheet structure was predominantly formed.

Sign in / Sign up

Export Citation Format

Share Document