The Amino Acid Composition of Bombyx mori Silk Fibroin and of Tussah Silk Fibroin

1955 ◽  
Vol 77 (14) ◽  
pp. 3908-3913 ◽  
Author(s):  
W. A. Schroeder ◽  
Lois M. Kay ◽  
Barry Lewis ◽  
Nancy Munger
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Bombyx Mori ◽  
Acid Composition ◽  
Silk Fibroin ◽  
Bombyx Mori Silk ◽  
Tussah Silk Fibroin

scholarly journals Amino acid identification of Bombyx mori fibroin cocoon as biomaterial using liquid chromatography/mass spectrometry

2020 ◽  
Vol 28 ◽  
pp. 02001
Author(s):  
Sartika Puspita ◽  
Siti Sunarintyas ◽  
Chairil Anwar ◽  
Ema Mulyawati ◽  
Marsetyawan HNE Soesatyo
Keyword(s):  
Mass Spectrometry ◽  
Mechanical Properties ◽  
Liquid Chromatography ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Bombyx Mori ◽  
Acid Composition ◽  
Liquid Chromatography Mass Spectrometry ◽  
Central Java ◽  
Chromatography Mass Spectrometry

A fibroin is a natural polymer that serves as a biomaterial because of the mechanical properties, biocompatible, biodegradable and amino acid composition. The mechanical properties of fibroin are influenced by crystalline structures of amino acid and are related to the amino acid composition. it can accelerate the wound healing because it promotes the proliferation of exposure tissue and inhibits inflammation. The study aimed to identify amino acid of Bombyx mori (B. mori) fibroin cocoon as biomaterial that was cultivated in Central Java Indonesia. Liquid Chromatography/Mass Spectrometry (LC/MS-Water, USA) was employed. This study found that fibroin of B. mori contains seventeen amino acids and the most abundant amino acid is L-Valin 4.81 % (mg kg–1).

Comparisons between gelatin-tussah silk fibroin/hydroxyapatite and gelatin-Bombyx mori silk fibroin/hydroxyapatite nano-composites for bone tissue engineering

RSC Advances ◽  
2015 ◽  
Vol 5 (93) ◽  
pp. 76526-76537 ◽  
Author(s):  
Jiabing Ran ◽  
Jingxiao Hu ◽  
Guanglin Sun ◽  
Si Chen ◽  
Li Chen ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Bone Tissue Engineering ◽  
Bombyx Mori ◽  
Bone Tissue ◽  
Silk Fibroin ◽  
Nano Composites ◽  
Enhancement Mechanism ◽  
Hydroxyapatite Composite ◽  
Bombyx Mori Silk ◽  
Tussah Silk Fibroin

Enhancement mechanism of tussah silk fibroin to gelatin-tussah silk fibroin/hydroxyapatite composite.

Three-Layered Sericins around the Silk Fibroin Fiber from Bombyx mori Cocoon and their Amino Acid Composition

2011 ◽  
Vol 175-176 ◽  
pp. 158-163 ◽  
Author(s):  
Yuan Jing Wang ◽  
Yu Qing Zhag
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Silk Fibroin ◽  
Reference Value ◽  
Solubility In Water ◽  
Silk Fibroin Fiber ◽  
Different Temperatures ◽  
Hydrophobic Amino Acids

The sericin coated around silk fibroin fiber is a natural protein-based polymer and presents a layered structure. According to the solubility in water under different temperatures and pressures, the sericin is divided into three parts of outer, middle and inner sericin layers accounting for 15%, 10.5% and 4.5% to the total silk protein (included sericin layers and fibroin fiber) in terms of the mass respectively. The partition within the sericin layer presents the relative proportions of 50%, 35% and 15% from the outer to inner layer. Furthermore, the differences of three layers in the amino acid composition are very significant. The non-polar amino acids in the outer, middle and inner sericins are gradually increased, in particular for alanine, which are accounted for 5.20, 6.13 and 11.58 mol% respectively; while its content jumps to 33.38 mol% in the silk fibroin fiber. Nevertheless, the polar amino acids, especially the neutral ones, are gradually decreased accounting for 39.34, 38.62 and 23.82 mol% respectively. Concentration of Serine drops most prominently, i.e. 28.00, 25.57 and 13.32 mol% respectively; while its content goes to 7.65 mol% in the silk fibroin fiber. On the other hand, the hydrophobic amino acids gradually increase and the hydrophilic amino acids go to oppsite way. These results indicate that the amino acid compositions of the outer and middle sericins are similar to each other, but those of the inner sericin are different from the others. The closer the sericin layer is to the silk fibroin fiber, the closer its amino acid composition is to that of the fibroin fiber. These obtained results are of important reference value for processing of silk sericin peptides and their applications in cosmetics, cell culture, healthy food and other areas.

Research Progress in Sequences Comparison and Crystal Structure of Silk Fibroin

2013 ◽  
Vol 664 ◽  
pp. 443-448 ◽  
Author(s):  
Bao Shan Yang ◽  
Jun Li ◽  
Hui Wang
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Silk Fibroin ◽  
Molecular Conformation ◽  
Research Progress ◽  
Sequence Characterization ◽  
Fibrous Protein ◽  
Unique Amino Acid ◽  
Sequence Characteristics

Silk fibroin is native fibrous protein extracted from silk. It has good mechanical properties because of its unique amino acid composition, complex of sequence characterization and the transform of crystalline structure under different condition. The characteristics of silk fibroin makes it better biological biocompatibility and biodegradability and have been used widely as biomaterials in the field of tissue engineering. Based on the introduction of its properties, the researches on the amino acid composition, sequence characteristics, molecular conformation, and its performance were reviewed in this paper.

EXTRACTION, PURIFICATION, AND PROPERTIES OF BACILLUS SOTTO TOXIN

1956 ◽  
Vol 2 (4) ◽  
pp. 416-426 ◽  
Author(s):  
T. A. Angus
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Bombyx Mori ◽  
Acid Composition ◽  
Toxic Protein ◽  
Crystalline Inclusions ◽  
Purification And Properties ◽  
Bombyx Mori L ◽  
Proteinaceous Toxin

A proteinaceous toxin has been extracted from sporulated cultures of Bacillus sotto Ishiwata. The toxin is similar in amino acid composition and biological activity to the crystalline inclusions produced by this microorganism and it appears that the toxic protein is associated with the crystals. The toxin is stable, and causes paralysis and death in the larvae of Bombyx mori L. (the silkworm) and other lepidopterous insects. The symptoms caused by the toxin are identical with those caused by ingestion of the whole microorganism.

Poly-L-alanylglycyl-L-alanylglycyl-L-serylglycine: A synthetic model of Bombyx mori Silk Fibroin

1966 ◽  
Vol 19 (3) ◽  
pp. 489 ◽  
Author(s):  
FHC Stewart
Keyword(s):  
Amino Acid ◽  
Bombyx Mori ◽  
Silk Fibroin ◽  
Amino Acid Residues ◽  
Protecting Group ◽  
Synthetic Model ◽  
Bombyx Mori Silk ◽  
Nitrophenyl Ester

The sequential polypeptide [Ala-Gly-Ala-Gly-Ser-Gly]n has been prepared by polymerization of a hexapeptide p-nitrophenyl ester. This polymer contains the repeating sequence of amino acid residues present in the crystalline regions of Bombyx mori silk fibroin. The o-nitrophenylsulphenyl amino-protecting group was used extensively in the synthesis of the hexapeptide active monomer from which the polypeptide was obtained.

Structural Study of Irregular Amino Acid Sequences in the Heavy Chain of Bombyx mori Silk Fibroin

2005 ◽  
Vol 6 (5) ◽  
pp. 2563-2569 ◽  
Author(s):  
Sung-Won Ha ◽  
Hanna S. Gracz ◽  
Alan E. Tonelli ◽  
Samuel M. Hudson
Keyword(s):  
Amino Acid ◽  
Bombyx Mori ◽  
Structural Study ◽  
Silk Fibroin ◽  
Heavy Chain ◽  
Amino Acid Sequences ◽  
Bombyx Mori Silk
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