Potential of a Novel Thermotolerant Lipase Bacillus stearothermophilus nr22 (Lip.nr-22) as Additive in High Temperature Operated-Neutral pH Liquid Detergent

Article Preview

Abstract:

Enzyme-added detergent must have the capability to operate at high temperature to support the enzyme proteins to clean soiled-fabrics at optimum conditions. Lipase from Bacillus stearothermophilus nr22 (Lip.nr-22) has improved the oil removal from soiled-cotton fabric by 38.8-51.4% in 4 types of local commercial detergents. The later was the oil removal from an unrevealed detergent. The optimum conditions were 108U/ml Lip.nr-22 in 0.1M, pH 7.0, washing temperature and washing time interval as 80°C and 40 min, respectively; shaking wash at 300 rpm and percentage of detergent concentration as 0.5. Lip.nr-22 is a very potential enzyme in high temperature-neutral pH operated laundry detergent formulations. It has exhibited a very excellent thermostability at 80°C, was very stable with surfactants, commercial detergents as well as with oxidizing agents (H2O2, NaBO3H2O and NaClO). Lip.nr-22 as additive in detergent formulation is a promise for better detergent formulation.

You might also be interested in these eBooks

Info:

Periodical:

Pages:

136-142

Citation:

Online since:

May 2017

Export:

Price:

Permissions CCC:

Permissions PLS:

Сopyright:

© 2017 Trans Tech Publications Ltd. All Rights Reserved

Share:

Citation:

* - Corresponding Author

[1] J. Adrie, Straathof,J. & Patrick,A. Applied Biocatalyst, Second Edition. CRC Press. (2003), p.5.

Google Scholar

[2] B. K. Sharma, Environmental Chemistry. GOEL Publishing House, Meerut (2007), p.335.

Google Scholar

[3] N. H. Nik Raikhan. Thermotolerant lipase from Geobacillus thermodenitrificans, the application in esterification and enantiomeric reactions. Ph. D Thesis. Universiti Sains Malaysia, Pulau Pinang Malaysia (2010).

DOI: 10.21315/mjms2020.27.3.2

Google Scholar

[4] A. Sugihara, Tani, T. and Tominaga, Y. Purification and characterization of a novel thermostable lipase from Bacillus sp. Journal of Biochemistry 109(2) (1991), pp.211-216.

Google Scholar

[5] N. H. Nik Raikhan. Production of hyperthermotolerant lipase from actinomycete Streptosporangium roseum. M. Sc. Thesis. Universiti Sains Malaysia, Penang, Malaysia (2003).

Google Scholar

[6] A. Mustranta, Forssell, P. and Poutanen, K. Applications of immobilized lipases to trans-esterification and esterification reactions in nonaqueous systems. Enzyme and Microbial Technology 15(2) (1993), pp.133-139.

DOI: 10.1016/0141-0229(93)90037-3

Google Scholar

[7] M. F. C. P., Jesus, Branco, R. N., Sant Anna Jr., G. L.,. Freire, D. M. G and Silva Jr., J. G. Penicillium restrictum lipases: A comparative study and characterization of enzymes with different degrees of purity. Brazilian Journal of Chemical Engineering 16(2) (1993).

DOI: 10.1590/s0104-66321999000200002

Google Scholar

[8] M. Chauhan, Chauhan, R. S. and Garlapati, V. K. Evaluation of a new lipase from Staphylococcus sp. for detergent additive capability. BioMed Research International Article ID 374967, (2013), 6 pages.

DOI: 10.1155/2013/374967

Google Scholar

[9] K.V. Sajna, Sukumaran, R. K. and Jayamurthy, H. Studies on biosurfactants from Pseudozyma sp. NII, 08165 and their potential application as laundry detergent additives. Biochemical Engineering Journal 78 (2013), pp.85-92.

DOI: 10.1016/j.bej.2012.12.014

Google Scholar

[10] P. Rathi, Saxena, R. K. and Gupta, R. A novel alkaline lipase from Burkholderia cepacia for detergent formulation. Process Biochemistry 37(2) (2001), pp.187-192.

DOI: 10.1016/s0032-9592(01)00200-x

Google Scholar

[11] U. Derewenda, Swenson, L. and Wei, L. Conformational liability of lipases observed in the absence of an oil-water interface: crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar. Journal of Lipid Research 35(3) (1994).

DOI: 10.2210/pdb1tib/pdb

Google Scholar

[12] J. A. C. Flipsen, Appel, A. C. M, van der Hijden, H. T. W. M. and Verrips, C. T. Mechanism of removal of immobilized triacylglycerol by lipolytic enzymes in a sequential laundry wash process. Enzyme and Microbial Technology 23(3-4) (1998).

DOI: 10.1016/s0141-0229(98)00050-7

Google Scholar

[13] N. P. Janaina, Juliana, A. B. C. and Gláucia, M. P. Characterization of alkaline lipase from Fusarium oxysporum and the effect of different surfactants and detergents on the enzyme activity. Brazilian Journal of Microbiology 37(4) (2006).

DOI: 10.1590/s1517-83822006000400019

Google Scholar

[14] K. V. Sajna, Sukumaran, R. K. and Jayamurthy, H. Studies on biosurfactants from Pseudozyma sp. NII, 08165 and their potential application as laundry detergent additives. Biochemical Engineering Journal 78 (2013), pp.85-92.

DOI: 10.1016/j.bej.2012.12.014

Google Scholar

[15] S. Grbavˇci´c, Bezbradica, D. and Izrael-ˇZivkovi´c, L. Production of lipase and protease from an indigenous Pseudomonasaeruginosa strain and their evaluation as detergent additives: compatibility study with detergent ingredients and washing performance. Bioresource Technology 102(24) (2011).

DOI: 10.1016/j.biortech.2011.09.076

Google Scholar