title: Enzymatic degradation of fibroin fiber by a fibroinolytic enzyme of Brevibacillus thermoruber YAS-1.
abstract: The employment of thermophiles and their enzymes is effective for the degradation of hard-to-degrade proteins. In this report, we describe the efficient degradation of fibroin, one major protein of silk fiber, by a thermophile and its enzymes. Brevibacillus thermoruber YAS-1, a thermophile which produces a proteinase with high action on fibroin fiber, was screened from samples obtained at the Manza hot springs, Gunma, Japan. The time course of fibroin degradation by the strain was investigated with a culture supernatant or concentrated enzyme sample. The breakdown of fibroin molecules was confirmed by the use of scanning electron microscopy, and the fibroin solubilized by the enzyme action was examined by amino acid composition analyses together with SDS-PAGE analysis. Herein, we demonstrate the significant degradation of fibroin fiber by strain YAS-1 and the potentials of its fibroinolytic enzyme(s).
authors: Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, Shimogamo, Sakyo, Kyoto 606-8522, Japan.
authors: Yasunori
authors: Y
authors: Suzuki
authors: Hiroshi
authors: H
authors: Matsui
authors: Yoshiyuki
authors: Y
authors: Tsujimoto
authors: Kunihiko
authors: K
authors: Watanabe
mesh_terms: D000818:Animals; D001407:Bacillus / Q000235:genetics / Q000378:metabolism*; D012831:Bombyx / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005349:Fibroins / Q000737:chemistry*; D007564:Japan; D008855:Microscopy, Electron, Scanning / Q000379:methods; D010447:Peptide Hydrolases / Q000737:chemistry; D010802:Phylogeny; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012336:RNA, Ribosomal, 16S / Q000737:chemistry; D020539:Sequence Analysis, Protein; D047011:Silk; D013997:Time Factors
chemical_list: D011506:Proteins; D012336:RNA, Ribosomal, 16S; D047011:Silk; D005349:Fibroins; D010447:Peptide Hydrolases