Extraction and Purification of Scleroprotein Obtained from Spiderweb

Department of Biotechnology, K. S. Rangasamy College of Technology, Tiruchengode- 637215, Namakkal, Tamil Nadu, India

^* Corresponding author: nithyam@ksrct.ac.in

Abstract

Spider silk belonged to the scleroprotein family; a group of structural proteins found in living organisms. Other members of this group include collagen, present in ligaments, and keratin, which forms fingernails, feathers, horns, and hoofs. Specific scleroproteins such as keratin, collagen, elastin, and fibroin were analysed in this study. The scleroprotein was extracted from spiderwebs, dialyzed, and purified using column chromatography. The total protein concentrations measured were 0.08 mg/ml in crude samples and 0.10 mg/ml after dialysis. Following column chromatography, the protein concentration increased to 0.15 mg/ml. The respective concentrations of keratin, collagen, and fibroin were 0.12 mg/ml, 0.11 mg/ml, and 0.08 mg/ml. Protein profiles were identified using SDS-PAGE with Bovine Serum Albumin as a standard. Keratin exhibited notable stimulatory effects on plant growth, specifically in Vigna radiata and Macrotyloma uniflorum. Treated Vigna radiata samples grew to an average height of 5.7 cm, compared to 4.1 cm in untreated controls. Similarly, treated Macrotyloma uniflorum plants reached a height of 6.3 cm, while untreated plants measured 4.4 cm after seven days of germination. The number of leaves also increased, with treated Macrotyloma uniflorum showing five leaves versus three in untreated samples, and treated Vigna radiata producing four leaves compared to two in untreated plants.