Feather degradation potential of Stenotrophomonas maltophilia KB13 and feather protein hydrolysate (FPH) mediated reduction of hexavalent chromium

• DOI: 10.1007/s13205-016-0370-5
• Publication Date: 2016-02-02T10:59:35Z
• Authors: Khushboo Bhange; Venkatesh Chaturvedi; Renu Bhatt
• Keywords: Keratinase; Hexavalent Chromium

An efficient keratinolytic strain of Stenorophomonas maltophilia KB13 was isolated from feather disposal site Bilaspur, Chhattisgarh, India. The could metabolize 10 g/l chicken feathers as sole source carbon and nitrogen. Soluble protein, amino acid, cysteine content were found to be maximum (690.6 ± 8.7, 688.9 9.12 21 0.36 µg/ml, respectively) at late logarithmic phase growth. Protease keratinase activity reached its level (103.26 7.09 178.5 9.10 U/ml) the 4th day incubation. protein hydrolysate (FPH) obtained after degradation utilized reduce hexavalent chromium. About 78.4 2.4 63.6 2.2 % reduction 50 100 mg/l Cr(VI), respectively, observed 60 min incubation with FPH. Further, there no effect autoclaved FPH on Cr(VI) indicating that any bacterial enzyme not involved in process. significantly inhibited by mm Hg2+ ions role sulfur-containing acids FTIR analysis confirmed chromium occurred due oxidation cystine. This study shows arising can employed a potential candidate for hexavalant