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Indian Journal of Pure & Applied Biosciences (IJPAB)
Year : 2014 , Volume 2, Issue 1
Page No. : 266-271
Article doi: : http://dx.doi.org/10.18782
Characterization of α-amylase producing Bacillus mycoides strains from Bay of Bengal, Visakhapatnam
K. Suribabu1*, T. Lalitha Govardhan1 and K. P. J. Hemalatha2
1PG Department Microbiology, Dr.Lankapalli Bullayya PG College, Visakhapatnam-530 013. A.P, India
2Department Microbiology, Andhra University, Visakhapatnam-530 003.A.P, India
*Corresponding Author E-mail: ksuribabu_sda@yahoo.com
ABSTRACT
Numerous marine microorganisms secrete enzymes which can provide new insights and understanding of
enzymes. Bacteria have been regarded as treasure of many useful enzymes viz., amylases, proteases,
lipases, hydrolases and reductases. Among them amylolytic enzymes have great biotechnological
applications and economic exploitations. The bacterial genus Bacillus proved to be an important source
of amylase in food, sewage treatment, textile and laundry industry. In the present study, α-amylase
producing Bacilli were isolated from coastal waters of Bay of Bengal, Visakhapatnam, were
characterized by employing various cultural, morphological and biochemical methods. Serially diluted
samples were cultured on Starch agar plates and incubated for 24 h at 370C, and then the plates were
flooded with Lugol’s solution. The colonies showing large halo zone of starch hydrolysis were selected
for further screening of Amylase activity. Three isolates of Bacillus mycoides; B. mycoides a1, B.
mycoides a3 and B. mycoides F5 were selected and identified. The enzyme activity was estimated by DNS
method for all isolates which were inoculated in nutrient broth and incubated at 370C for 24 hours. The
Amylase activity of B. mycoides F5 was found to be maximum, 1023 μg/ml and three isolated B. mycoides
a1, B. mycoides a3 and B. mycoides F5 showed within a range of 800 to 1100 μg/ml.
Keywords: Bacillus mycoides,α-amylase, Cultural, Morphological, Biochemical characterization.
Full Text : PDF; Journal doi : http://dx.doi.org/10.18782
Cite this article:
Int. J. Pure App. Biosci. 2 (1): 266-271 (2014)
