지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제23권 제8호
- 발행연도
- 2013.1
- 수록면
- 1,133 - 1,139 (7page)
이용수
초록· 키워드
오류제보하기
Enzymatic decomposition of gelatin layers on used X-ray films and repeated utilization of the enzyme for potential application in silver recovery were investigated using keratinolytic serine proteases from Purpureocillium lilacinum LPS # 876. At pH 9.0, the enzymatic reaction was enhanced by the increase of enzyme concentration or by the increase of the temperature up to 60oC. Under the conditions of 6.9 U/ml, 60oC, and pH 9.0, hydrolysis of the gelatin layers and the resulting release of silver particles were achieved within 6 min. The protective effect of polyols against thermal denaturation was investigated. The presence of glycerol and propylene glycol increased enzyme stability. When the reusability of the enzyme for gelatin hydrolysis was tested, it could be seen that it could be effectively reused for more cycles when glycerol was added, compared with the enzyme without protective agents. The results of these repeated treatments suggested that a continuous process of recycling silver from used X-ray is feasible. Keeping in mind that recycling is (at the present time) needed and imperative, it can be remarked that, in this research, three wastes were successfully used: hair waste in order to produce serine proteases; glycerol in order to enhance enzyme thermal stability; and used Xray films in order to recover silver and PET films.
목차
등록된 정보가 없습니다.
참고문헌 (16)
참고문헌 신청
Bayoudh A / 2000 / Purification and characterization of an alkaline protease from Pseudomonas aeruginosa MN1 / J. Ind. Microbiol. Biotechnol 24 : 291 ~ 295
Bhosale SH / 1995 / Thermostability of high-activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20) / Enzyme Microb. Technol 17 : 136 ~ 139
Cavello IA / 2012 / Bioprocessing of “Hair Waste” by Paecilomyces lilacinus as a source of a bleachstable, alkaline, and thermostable keratinase with potential application
Christian GD / 1994 / Analytical Chemistry, In John Wiley and Sons / John Wiley and Sons : 683 ~ 686
Cobos A / 2003 / Effect of polyhydroxylic cosolvents on the thermostability and activity of xylanase from Trichoderma reesei QM 9414 / Enzyme Microb. Technol 33 : 810 ~ 818
Bhosale SH / 1995 / Thermostability of high-activity alkaline protease from Conidiobolus coronatus (NCL 86.8.20) / Enzyme Microb. Technol 17 : 136 ~ 139
Cavello IA / 2012 / Bioprocessing of “Hair Waste” by Paecilomyces lilacinus as a source of a bleachstable, alkaline, and thermostable keratinase with potential application
Christian GD / 1994 / Analytical Chemistry, In John Wiley and Sons / John Wiley and Sons : 683 ~ 686
Cobos A / 2003 / Effect of polyhydroxylic cosolvents on the thermostability and activity of xylanase from Trichoderma reesei QM 9414 / Enzyme Microb. Technol 33 : 810 ~ 818
이 논문의 저자 정보
최근 본 자료
댓글(0)
0