The silk proteins, sericin and fibroin in silkworm, Bombyx mori

نویسنده

  • Nirmal Kumar
چکیده

The domesticated silkworm, Bombyx mori Linn., a lepidopteran molecular model and an important economic insect that are emerging as an ideal molecular genetic resource for solving a broad range of biological problems. The silkworm, B. mori produces massive amount of silk proteins during the final stage of larval development. These proteins are stored in the middle silk gland and they are discharged through the anterior duct and spinneret, at the end of the fifth instar. Two kinds of silk proteins have been distinguished as major components of silk cocoons, the first being fibroin, a fibrous protein composed of heavy (H) chain, Light (L) chain and glycoprotein linked by disulfide bonds and the second being sericin a natural macromolecular protein, serving as an adhesive to unite fibroin for making silk cocoons of silkworm, B. mori. Recently, silkworm is being used as biofactory for the production of useful protein using the silk gland, which has promoted the technological development in sericulture. With the above background silkworm can be classified as a value added biomaterial for medical application, application of silk protein fibroin and sericin as a biomaterial and other seri-byproducts. The present paper overviews some important studies carried out on sericin and fibroin of silkworm, Bombyx mori Linn.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The silk proteins, sericin and fibroin in silkworm, Bombyx mori Linn., - a review

The domesticated silkworm, Bombyx mori Linn., a lepidopteran molecular model and an important economic insect that are emerging as an ideal molecular genetic resource for solving a broad range of biological problems. The silkworm, B. mori produces massive amount of silk proteins during the final stage of larval development. These proteins are stored in the middle silk gland and they are dischar...

متن کامل

The silk proteins, sericin and fibroin in silkworm, Bombyx mori Linn., - a review

The domesticated silkworm, Bombyx mori Linn., a lepidopteran molecular model and an important economic insect that are emerging as an ideal molecular genetic resource for solving a broad range of biological problems. The silkworm, B. mori produces massive amount of silk proteins during the final stage of larval development. These proteins are stored in the middle silk gland and they are dischar...

متن کامل

Evaluation of silk sericin as a biomaterial: in vitro growth of human corneal limbal epithelial cells on Bombyx mori sericin membranes

Sericin and fibroin are the two major proteins in the silk fibre produced by the domesticated silkworm, Bombyx mori. Fibroin has been extensively investigated as a biomaterial. We have previously shown that fibroin can function successfully as a substratum for growing cells of the eye. Sericin has been so far neglected as a biomaterial because of suspected allergenic activity. However, this mis...

متن کامل

LIM-homeodomain transcription factor Awh is a key component activating all three fibroin genes, fibH, fibL and fhx, in the silk gland of the silkworm, Bombyx mori.

In the silkworm Bombyx mori, three fibroin genes, fibroin-heavy-chain (fibH), fibroin-light-chain (fibL) and fibrohexamerin (fhx), are coexpressed only in the posterior silk gland (PSG) cells, while the sericin genes encoding silk glue proteins are expressed in the middle silk gland (MSG) cells. Silk gland factor-2 (SGF-2) is a PSG-specific activator complex of fibH, composed of a LIM-homeodoma...

متن کامل

Transcriptome Sequencing and Positive Selected Genes Analysis of Bombyx mandarina

The wild silkworm Bombyx mandarina is widely believed to be an ancestor of the domesticated silkworm, Bombyx mori. Silkworms are often used as a model for studying the mechanism of species domestication. Here, we performed transcriptome sequencing of the wild silkworm using an Illumina HiSeq2000 platform. We produced 100,004,078 high-quality reads and assembled them into 50,773 contigs with an ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2005