Kinetic studies on recombinant stem bromelain - Advances in Enzyme Research

AER > Vol.1 No.3, September 2013

Advances in Enzyme Research

Volume 1, Issue 3 (September 2013)

ISSN Print: 2328-4846 ISSN Online: 2328-4854

Google-based Impact Factor: 0.77 Citations

Kinetic studies on recombinant stem bromelain ()

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DOI: 10.4236/aer.2013.13006 7,942 Downloads 14,884 Views Citations

Author(s)

Muntari Bala, Maizirwan Mel, Mohamed Saedi Jami, Azura Amid, Hamzah Mohd Salleh

Affiliation(s)

Bioprocess and Molecular Engineering Research Unit, Department of Biotechnology Engineering, International Islamic University Malaysia, Kuala Lumpur, Malaysia.
International Institute for Halal Research & Training (INHART) International Islamic University Malaysia, Kuala Lumpur, Malaysia.

ABSTRACT

Stem bromelain is a plant thiol protease with several industrial and therapeutic applications. This current work presents kinetic studies of recombinant bromelain (recBM) expressed in Escherichia coli BL21-AI on foursynthetic substrates, N-α-carbobenzoxy-L-alanyl-p-nitrophenylester (ZANPE), N-α-carbobenzoxy-L-arginyl-L-ar-ginine-p-nitroanilide (ZAANA), N-α-carbobenzo-xy-L-phenylalanyl-L-valyl-L-arginine-p-nitroanili-de (ZPVANA) and L-pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide (PFLNA). Hydrolytic activities of recBM at various pH and temperature conditions were compared to that of commercial bromelain (cBM). Both enzymes demonstrated high activities at 45^oC and pH 5 - 8 for recBM and pH 6 - 8 for cBM. recBM showed marginally lower Kmand slightly higher kcat/Kmfor ZAANA, ZANPE and ZPVANA in comparison to cBM.trans Epoxysuccinyl-L-leucylamido {4- guanidino}butane (E-64) severely affected recBM and cBM hydrolysis of the synthetic substrates by competitive inhibition with Kivalues of 3.6 - 5.1 μM and 5.5 - 6.9 μM for recBM and cBM, respectively. The evaluated properties of recBM including temperature and pH optima, substrate specificity and sensitivity to inhibitors or activators, satisfy the requisites required for food industries.

KEYWORDS

Protease; Recombinant Bromelain; Substrates; Inhibitors; Activators

Share and Cite:

Bala, M. , Mel, M. , Saedi Jami, M. , Amid, A. and Mohd Salleh, H. (2013) Kinetic studies on recombinant stem bromelain. Advances in Enzyme Research, 1, 52-60. doi: 10.4236/aer.2013.13006.

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