• International Journal of Industrial Entomology and Biomaterials
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• 제4권1호
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• pp.1-4
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• 2002

Silk proteins consist of two major proteins, fibroin and sericin. There is currently an enormous reawakening of interest in these silk proteins as a biomaterial due to their mechanical and biological properties based on the detailed findings. Novel method for determination of the crystalline structure of silk proteins in an atomic level using nuclear magnetic resonance (NMR) was reviewed. Recent application of silks to biomaterials and prospects for future were discussed.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2001년도 추계학술발표대회
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• pp.719-722
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• 2001

Silk proteins from Nephila clavipes are fibrous proteins containing repetitive sequences with both crystalline and amorphous domains. In order to obtain high-level production of silk protein, the synthetic genes had 16 contiguous units of the consensus repeat sequence of the silk protein were expressed in Escherichia coli BL21(DE3) under the strong inducible T7 promoter. For production of recombinant silk protein in large amounts, pH-stat fed-batch cultures were carried out. The recombinant silk protein was produced as soluble forms in E. coli, and the recombinant silk protein content was as high as 11% of the total protein. When cells were induced at $OD_{600}$ of 60, the amount of silk protein produced was 6.49 g/L. After simple purification steps, 9.2 mg of silk protein that was more than 80% pure was obtained from a 50 mL culture, and the recovery yield was 26.3%.

• Maxillofacial Plastic and Reconstructive Surgery
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• 제40권
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• pp.10.1-10.6
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• 2018

Background: The objective of this study was to evaluate the changes in gene expression after incubation of cells with proteins released from different silk mat layers. Methods: A silk cocoon from Bombyx mori was separated into four layers of equal thickness. The layers were numbered from 1 to 4 (from the inner to the outer layer). The proteins were released by sonication of a silk mat layer in normal saline. The concentration of proteins was determined by spectrophotometry. They were incubated with RAW264.7 cells, and changes in the expression of genes were evaluated by cDNA microarray analysis and quantitative reverse transcriptase-polymerase chain reaction (qRT-PCR). Results: Layer 1 and 4 groups had higher protein concentrations compared to those in layer 2 and 3 groups. The genes associated with inflammation and angiogenesis showed significantly higher expression in layer 1 and 4 groups. The results of qRT-PCR were in agreement with those of the cDNA microarray analysis. Conclusions: The silk mat from the middle portion of the silkworm cocoon yielded a lower protein release and caused an insignificant change in the expression of genes that are associated with inflammation and angiogenesis.

• Applied Microscopy
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• 제50권
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• pp.16.1-16.11
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• 2020

Silk is produced by a variety of insects, but only silk made by terrestrial arthropods has been examined in detail. To fill the gap, this study was designed to understand the silk spinning system of aquatic insect. The larvae of caddis flies, Hydatophylax nigrovittatus produce silk through a pair of labial silk glands and use raw silk to protect themselves in the aquatic environment. The result of this study clearly shows that although silk fibers are made under aquatic conditions, the cellular silk production system is quite similar to that of terrestrial arthropods. Typically, silk production in caddisworm has been achieved by two independent processes in the silk glands. This includes the synthesis of silk fibroin in the posterior region, the production of adhesive glycoproteins in the anterior region, which are ultimately accumulated into functional silk dope and converted to a silk ribbon coated with gluey substances. At the cellular level, each substance of fibroin and glycoprotein is specifically synthesized at different locations, and then transported from the rough ER to the Golgi apparatus as transport vesicles, respectively. Thereafter, the secretory vesicles gradually increase in size by vesicular fusion, forming larger secretory granules containing specific proteins. It was found that these granules eventually migrate to the apical membrane and are exocytosed into the lumen by a mechanism of merocrine secretion.

• International Journal of Industrial Entomology and Biomaterials
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• 제17권1호
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• pp.109-113
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• 2008

Realizing the scope of utilizing by-products of silk cocoons by applying appropriate methods is the immediate crave to optimize returns. The nutritive value of pupae suits for human diet, feed for poultry, carps, fish, rabbits, piggery and dogs. The pupal skin, fat, oil, cocoon palade have applications in oleo chemical, soap, glycerin, cosmetic, artificial fibres, membranes and n-triacontanol isolation. The pupal proteins Chitin, Shinki fibroin, Serrapeptidase, glucosamine are latent precursors of post surgical, anti-carcinogenic, anti-inflammative, anti-bacterial, anti-histaminic, gastric, hepatitis, pancreatitis, leukocytopenia, neurological, ophthalmic, blood pressure, cardiac and diabetic medicines and for preparation of vitamins A, E and K. The silk and its proteins sericin and fibroin are potentially used for wound healing, diabetes, impotence, sinusitis, arthritis, edema, cystitis, epididymitis, tissue regeneration, cancer, post-surgical trauma and used as anti-oxidatives, bio-adhesives, ultra violet screens and bio-active textiles. The waste cocoons can be used in making art crafts like garlands, carpets, overcoats, decoratives and greeting cards. The in-depth research towards utility optimization and make aware this reality to sericulturists, reelers, weavers, traders, entrepreneurs, policy makers etc., is the upright want of the today's Sericulture industry.

• 한국잠사학회:학술대회논문집
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• 한국잠사학회 2003년도 제46회 춘계 학술연구 발표회
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• pp.59-59
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• 2003

Silk sericin (SS) is one of essential components of cocoon filament, comprising granular and high molecular proteins with adhesive and gelatin-like characteristics. Silk fibroin (SF), another main component of cocoon filament, has been investigated by many researchers due to its good physicochenucal properties. Recently, Nam and Park reported that the effect of alcohol addition into the SF solution on the morphology and structural charateristics of SF. (omitted)

• 한국섬유공학회:학술대회논문집
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• 한국섬유공학회 2001년도 가을 학술발표회 논문집
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• pp.392-396
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• 2001

Natural silk is formed by two proteins ; the crystalline fibroin (inside the silk thread) and amorphous sericin (as a tube outside the thread). The degumming process is used th eliminate the external sericin prior to dyeing ： generally it makes use of soaps at pH 10. (omitted)

• 한국잠사곤충학회지
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• 제53권2호
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• pp.92-96
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• 2015

본 연구는 장려 품종 누에고치로부터 실크 세리신과 실크 피브로인으로 분리하여 이들 단백질을 세포 첨가제로 개발하기 위하여 수행되었다. 장려품종 누에고치를 고온 고압기를 통하여 실크 세리신을 먼저 추출하였으며, 남겨진 실크 피브로인을 이용하여 시간별로 용해하여 품종별 실크 피브로인을 얻었다. 이들 실크 세리신과 실크 피브로인을 이용하여 세포 독성, 세포 증식 및 분열 관련 유전자 발현 분석을 확인하였다. 먼저, 누에고치의 특성을 분석하기 위하여 공극률을 측정하였다. 공극률은 금옥잠 누에고치의 경우 84.71%, 대성잠 81.58%, 백옥잠 73.23%의 공극률 값이 나타났다. 분자량 차이에 있어서 실크 세리신은 품종의 영향이 크지 않았으나 실크 피브로인의 경우, 금옥잠은 5시간의 장시간의 용해에도 불구하고 100 kDa 이상의 큰 분자량을 나타내었다. 장려품종 누에를 사용하여 제조된 실크 세리신과 실크 피브로인을 이용하여 세포 증식 실험을 하였으며 백옥잠으로부터 얻은 실크 세리신의 경우 농도에 따라 유의적으로 세포 증식 효과가 나타났으며, 금옥잠으로부터 얻은 실크 피브로인의 경우 5시간 용해 시 세포 증식에 있어서 가장 우수한 결과를 보였다. 또한, 백옥잠 실크 세리신 처리 결과 세포 증식 관련 유전자의 발현수준이 증가됨을 확인할 수 있었다.

• 한국잠사학회:학술대회논문집
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• 한국잠사학회 2001년도 제44회 추계 학술연구 발표회
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• pp.24-29
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• 2001

no Abstract, See Full Text

• Animal cells and systems
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• 제6권4호
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• pp.327-333
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• 2002

Among the silk glands in the black widow spider Latrodectus mactans, the ampullate one is the most predominant gland in both sexes, and is com-posed of three functional parts - excretory duct, storage ampulla and convoluted tail regions. This experiment was performed using mechanical pulling stimulation with electric motor equipment to reveal a correlation between silk usage and silk producing system in this poisonous spider. The mature secretory products in glandular epithelium are closely packed and appear as electron-opaque spherical vesicles. A part of the vesicles with fine fibrillar paracrystalline texture seems to store some proteins which will function at the time of final assembly into fibrils. Most of the secretory silk products which originated from the rough endoplasmic reticula of the glandular epithelial cells are grown by fusion with surrounding small vesi-cles. However, the Golgi complex does not seem to play an important role in this process of secretion. According to progressive maturation of secre-tory silk product, these granules are progressively filled with a fine fibrillar material, and thus appear much more electron-dense than those of earlier states. When the secretory product is extruded from the glandular cavity, the epithelium is rapidly changed to a thinner layer of tall columnar cells with less definitive cell membranes. After extruding there ave a few secre-tory droplets within these cells, thus causing this region to stain much lighter.