Degradation of raw feather by a novel high molecular weight extracellular protease from newly isolated Bacillus cereus DCUW

Ghosh, Abhrajyoti; Chakrabarti, Krishanu; Chattopadhyay, Dhrubajyoti

doi:10.1007/s10295-008-0354-5

Cited by 63 publications

(44 citation statements)

References 35 publications

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“…A wide range of variations can be observed in fungal keratinases (18-200 kDa) [36]. Even though the present study was contradictory to the above reports [3,4,34] later major variations are existing even among the fungal keratinases are confirmed with the report [36]. …”

contrasting

confidence: 56%

Bio-prospecting of marine-derived fungi with special reference to production of keratinase enzyme - A need-based optimization study

2018

J App Biol Biotech

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Keratin derived from poultry, and other keratinous waste remains a headache to the human society and also to the nature. Marine fungi -an untapped resource to be exploited specifically for the production of keratinase. In this connection, marine sediment samples were randomly collected from Kovalam located along the south west coast of Tamil Nadu. Two marine-derived fungi were isolated from the sediment samples. The internal transcribed spacer region of the isolates was sequenced, submitted to the GenBank and an individual accession number obtained for Colletotrichum capsici (KY817475) and Curvularia lunata (KY828216). Keratinase enzyme was produced with C. capsici and C. lunata at pH 8.5, and total protein was estimated. The amount of protein produced by C. capsici was found to be 0.91 mg/ml and by C. lunata was 1.06 mg/ml. The molecular weight of keratinase was determined as 35kDa. Four parameters through pH, concentration of feather meal, carbon source, and nitrogen source were optimized during the present study. Keratinase production media inoculated with C. capsici and C. lunata exhibit OD max with respect to feather meal concentration and corresponding OD was 1.264 mg/ml and 0.639 mg/ml. The OD max for C. capsici and C. lunata supplemented with maltose as carbon source was 1.281 mg/ml and 1.426 mg/ml. The OD max for C. capsici and C. lunata supplemented with yeast extract as nitrogen source and corresponding OD was 1.858 mg/ml and 1.613 mg/ml. Thus, we conclude that marine-derived fungi C. capsici and C. lunata are potential producers of ecovaluable keratinase which could be used up to treat the ecological burden created by keratinous waste. INTRODUCTIONSoil-borne microfungi are reported to synthesize a wide variety of hydrolytic enzymes. Still several species are exploited in the industries toward the production of industrially important enzymes such as cellulase, pectinase, carbohydrase, and lipase. A unique class of enzyme called keratinase produced by microfungi population has both biotechnological, biomedical potentials, and ecological benefits. Some clinically important pathogenic dermatophytes such as Trichophyton spp.[1] produce this enzyme to invade the skin tissues. On the other hand, the microbial keratinase has ecovaluable role since it is being applied in the bioconversion of poultry and other keratinous waste. For this purpose keratinases trapped from Streptomyces spp. [2,3] and Bacillus spp. [4,5] have been investigated. Around 24 billion chickens were killed annually consequently 8.5 billion tone of poultry feather *Corresponding Author: Samuel Ponpandian, Department of Biotechnology, Ayya Nadar Janaki Ammal College, Sivakasi, Tamil Nadu, India. Email: drsamuelponpandian@rediffmail.com waste are generated. As per a recent citation from India's leading newspaper that our country alone contributes 350 million tone of poultry waste. Discarded feather causes several ailments to human beings such as chlorosis, mycoplasmosis, and fowl cholera [6]. Poultry waste drenched during the ...

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confidence: 56%

Bio-prospecting of marine-derived fungi with special reference to production of keratinase enzyme - A need-based optimization study

2018

J App Biol Biotech

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“…In our previous work on feather-degrading protease (Ghosh et al, 2008), we found 70±10 kDa protein bands during purification studies. Moreover, during the native protein purification, we found that several smaller fragments (both proteolytically active and inactive) were generated from the purified protease.…”

Section: Expression and Characterization Of Deletion Mutantsmentioning

confidence: 76%

“…The present analysis suggests that this C-terminal domain is probably responsible for the substrate binding via protein-protein interactions. Previously we have shown that this protease could degrade feather residues (Ghosh et al, 2008). In the present study, the feather keratin-binding assay was designed to check whether the C-terminal domain specifically binds to feather.…”

Section: Full-length Sequencing Of Vpr Gene and Domain Analysismentioning

confidence: 99%

Cloning of feather-degrading minor extracellular protease from Bacillus cereus DCUW: dissection of the structural domains

2009

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Bacterial extracellular proteases play an important role in cell survival and cell-cell communication. A high-molecular-mass minor extracellular protease (Vpr) from a featherdegrading bacterium, Bacillus cereus DCUW, has been reported by our laboratory. In the present study, we cloned and expressed Vpr in Escherichia coli. Complete nucleotide sequencing of this gene predicted that the protease is a member of the serine protease family, and SMART domain analysis revealed that the protease consists of an N-terminal signal sequence for secretion, a subtilisin_N sequence that is a signature for N-terminal processing, a catalytic S_8 peptidase domain, and finally a long C-terminal protease-associated (PA) region containing nine intrinsically disordered subdomains. Four truncated constructs of the Vpr protease were cloned and expressed in E. coli. We found that the catalytic domain (amino acid residues 172-583) is sufficient for protease activity. Maturation of the Vpr protease needed both N-terminal and Cterminal processing. We have demonstrated that the oligomerization property is associated with the C-terminal protease-associated domain and also shown that the substrate-binding specificity to raw feather resides in this domain.

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“…Kecernaan yang rendah disebabkan karena adanya kandungan kolagen pada MBM (Ravindran et al, 2005) dan keratin pada HCFM (Ghosh et al, 2008) …”

Section: Pendahuluanunclassified

Penggunaan Protease Dalam Pakan Yang Menggunakan Limbah Pertanian-Peternakan Untuk Meningkatkan Kinerja Pertumbuhan Ayam Broiler

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et al. 2017

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INTISARIPenelitian ini bertujuan untuk mengetahui pengaruh penambahan protease dalam pakan yang menggunakan limbah pertanian-peternakan terhadap konsumsi pakan, pertambahan bobot badan, konversi pakan (FCR), dan bobot badan ayam broiler fase starter, fase finisher, dan keseluruhan umur. Penelitian dilakukan selama 35 hari menggunakan 4.092 ekor ayam. Protease komersial yang dipergunakan dihasilkan oleh Bacillus licheniformis yang berbasis keratinase. Perlakuan yang diberikan berupa: pakan basal tanpa penambahan enzim (P1); P1 + 0,05% protease (P2); pakan basal dengan penambahan distiller's dried grain with soluble (DDGS) dan meat bone meal (MBM) (P3); P3 + 0,05% protease (P4); pakan basal dengan penambahan DDGS dan hydrolized chicken feather meal (HCFM) (P5); serta P5 + 0,05% protease (P6). Data yang diperoleh dianalisis variasi rancangan acak lengkap pola searah. Perbedaan antar perlakuan diuji lanjut menggunakan uji kontras ortogonal. Hasil penelitian menunjukkan bahwa penggunaan enzim protease pada pakan yang menggunakan limbah pertanianpeternakan tidak mempengaruhi kinerja pertumbuhan ayam pada fase starter dan keseluruhan umur, namun menurunkan nilai pertambahan bobot badan dan FCR fase finisher (P<0,05) pada pakan yang menggunakan MBM. Kesimpulan dari penelitian yang telah dilakukan bahwa enzim protease yang digunakan dalam penelitian ini lebih bekerja pada pakan basal yang menggunakan HCFM dan DDGS daripada MBM dan DDGS. ABSTRACT This study was aimed to determine the effects of protease supplementation in diets with agricultural-livestock by products on the feed intake, nett gain, feed conversion ratio

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Degradation of raw feather by a novel high molecular weight extracellular protease from newly isolated Bacillus cereus DCUW

Cited by 63 publications

References 35 publications

Bio-prospecting of marine-derived fungi with special reference to production of keratinase enzyme - A need-based optimization study

Bio-prospecting of marine-derived fungi with special reference to production of keratinase enzyme - A need-based optimization study

Cloning of feather-degrading minor extracellular protease from Bacillus cereus DCUW: dissection of the structural domains

Penggunaan Protease Dalam Pakan Yang Menggunakan Limbah Pertanian-Peternakan Untuk Meningkatkan Kinerja Pertumbuhan Ayam Broiler

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