PRODUCTION OF ALPHA AMYLASES BY ASPERGILLUS NIGER USING CHEAPERSUBSTRATES EMPLOYING SOLID STATE FERMENTATION
Jahir Alam Khan, Sachin Sopan Yadav
Abstract
Jahir Alam Khan, Sachin Sopan Yadav
Abstract
Four fungal isolates from soil were screened for alpha amylase production and the isolate MJSU1101 later identified as Aspergillus niger was found to have best activity among all the four isolates. Growth of Aspergillus niger was found to be optimum at 28°C and pH 6.2. SSF was carried out using four substrates namely wheat bran, rice husk, vegetable waste (potato, tomato, brinjal) and banana peel. Alpha amylase produced using all the four substrates was having good activity but wheat bran as a substrate was the best giving an activity of 0.08U/ml/min followed by vegetable waste (0.06U/ml/min), banana peels (0.05U/ml/min) and rice husk (0.045U/ml/min).
OpenAlex reports 35 citations for this work. Citation counts describe recorded attention and do not establish research quality.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
Four fungal isolates from soil were screened for alpha amylase production and the isolate MJSU1101 later identified as Aspergillus niger was found to have best activity among all the four isolates. Growth of Aspergillus niger was found to be optimum at 28°C and pH 6.2. SSF was carried out using four substrates namely wheat bran, rice husk, vegetable waste (potato, tomato, brinjal) and banana peel. Alpha amylase produced using all the four substrates was having good activity but wheat bran as a substrate was the best giving an activity of 0.08U/ml/min followed by vegetable waste (0.06U/ml/min), banana peels (0.05U/ml/min) and rice husk (0.045U/ml/min).
Key concepts: Aspergillus niger, Husk, Bran, Solid-state fermentation, Food science, Fermentation, Alpha-amylase, Chemistry