Protease Production by Aspergillus oryzae in Solid-State Fennentation Utilizing Coffee By-Products.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
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Relation |
http://ir.cftri.com/12782/
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Title |
Protease Production by Aspergillus oryzae in Solid-State
Fennentation Utilizing Coffee By-Products.
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Creator |
Pushpa, S. Murthy
Madhava Naidu, M. |
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Subject |
04 Fermentation Technology
04 Coffee 07 Waste utilization |
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Description |
Aspergillus oryzae CFR305 was isolated from coffee residues and studied for protease production
using coffee substrates lUlder solid-state fermentation. Coffee cherry husk was fOWld to be suitable substrate
for protease production. The influence of process parameters such as temperature, pH, moisture, particle size,
inoculum size, additives and pretreatments of substrates were evaluated. Maximum protease production of
12236 U/gds was obtained on pretreated coffee cherry husk by steam. The protease was partially purified and
characterized. The enzyme was purified 33.76 fold by ammonium sulphate precipitation and ion exchange
chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) indicates that the
purified protease is a monomeric enzyme with a molecular mass of ~35 kDa. The enzyme is a serine protease as
indicated by its inhibition studies. The protease enzyme showed maximum activity at pH 10 at 60°C. Thus, the
alkaline serine protease indicate their use as additives in industry and also states the importance of SSF for the
production of protease using coffee cherry husk as substrate, which offer significance benefit due to abundant
availability and economy. This is the first report on production of protease using coffee by-products.
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Date |
2010
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Type |
Article
PeerReviewed |
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Format |
pdf
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Language |
en
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Identifier |
http://ir.cftri.com/12782/1/World%20Appl%20Sci%20Jl%208%282%29%202010%20199-.pdf
Pushpa, S. Murthy and Madhava Naidu, M. (2010) Protease Production by Aspergillus oryzae in Solid-State Fennentation Utilizing Coffee By-Products. World Applied Sciences Journal, 18 (2). pp. 199-205. |
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