Journal of Applied & Environmental Microbiology
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Journal of Applied & Environmental Microbiology. 2014, 2(2), 37-41
DOI: 10.12691/jaem-2-2-1
Open AccessArticle

Bovine Serum Albumin a Potential Thermostabilizer: a Study on α-Amylase

Vijay Kishore1, , Sangeetha Gowda K. R.2, Swati Krishna1, Kusha Sharma1, Rashmi M.1 and Nishita K. P.3

1Department of Biotechnology, Sapthagiri College of Engineering, Bangalore 560 057, India

2Department of Studies and Research in Industrial Chemistry, School of Chemical Sciences, Kuvempu University, Shankaraghatta 577 451, India

3Fermentation Technology and Bio-Engineering Department, CFTRI, Mysore 570 020, India

Pub. Date: February 20, 2014

Cite this paper:
Vijay Kishore, Sangeetha Gowda K. R., Swati Krishna, Kusha Sharma, Rashmi M. and Nishita K. P.. Bovine Serum Albumin a Potential Thermostabilizer: a Study on α-Amylase. Journal of Applied & Environmental Microbiology. 2014; 2(2):37-41. doi: 10.12691/jaem-2-2-1


Bovine serum albumin (BSA) as a modifier was used with glutaraldehyde as a binder to study the activity and thermal stability of α-amylase. The optimum temperature of the enzyme was found to be 50C ± 2C. Further increase in temperature resulted in irreversible thermal inactivation of the enzyme. On modification of the enzyme with BSA, the rate of thermal inactivation was found to be significantly reduced. BSA modified α-amylase was found to retain its activity at 80C even after 3 h of incubation. The apparent thermal inactivation energy (Ed) of α-amylase was found to be significantly increased on modification with BSA. The half-life of BSA modified α-amylase at both 70C and 80C was found to be 2.5 times higher than the native α-amylase. Thermodynamic parameters, ΔH, ΔS and ΔG, were determined as a function of temperature. The kinetic constants Km and Vmax, using starch as substrate, were determined to study the effect of BSA conjugation on α-amylase.

bovine serum albumin α-amylase half-life modification thermal inactivation

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