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Optimization of Keratinase Production by Bacillus circulans BE-1 Using Alkali Pre-Treated Substrate
Bibliografi
Author:
CIOMAS, JENNIFER K
;
Purwadaria, Tresnawati
(Advisor);
Suhartono, Maggy Thenawidjaja
(Advisor)
Topik:
Keratinase
;
Optimization
;
Pre-Treatment
;
Bacillus circulans
Bahasa:
(EN )
Penerbit:
Fakultas Teknobiologi Unika Atma Jaya (Faculty of Biotechnology Atma Jaya Catholic University of Indonesia)
Tempat Terbit:
Jakarta
Tahun Terbit:
2008
Jenis:
Theses - Undergraduate Thesis
Fulltext:
Jennifer's Undergraduate Thesis.pdf
(453.02KB;
30 download
)
Ketersediaan
Perpustakaan Pusat (Semanggi)
Nomor Panggil:
FTB-127
Non-tandon:
tidak ada
Tandon:
1
Lihat Detail Induk
Abstract
Applications of keratin degrading microorganisms and their enzymes in the industry have attracted a great deal of attention. The enzyme was applied to remediate poultry feather waste. In this study, the optimal pre-treatment of substrate, substrate concentration, and incubation time for keratinase production by Bacillus circulans BE-1 were determined. The first experiment was conducted to determine the optimal treatment of substrate, the main factor was NaOH concentration (0.5, 0.1%) while the sub factor was boiling time (5 and 20 minutes). The next experiment mimiced the first experiment except that the substrate was treated with lower concentration of NaOH (0.100- 0.025%). The highest activity (228 U/ml) and specific activity (1161 U/mg) were observed in 0.025% NaOH concentration with 20 minutes boiling time treatment (P<0.01). The next experiment was designed to determine optimal substrate concentration (1.0, 1.5, 2.0, and 2.5%) and incubation time (4 and 7 days). Optimal substrate concentration was 1% (P<0.05), while longer incubation time did not significantly affect the enzyme production. Optimal incubation time was 4 days regarding economical value. The molecular fractions of crude enzyme in degrading kinds of protein were also determined. There were different fractions of keratinase that able to hydrolyze various protein substrates. Chicken feather powder was degraded by 25-27 kD and 20-22 kD molecular fractions of keratinase.
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