Response Surface Methodology as An Approach to Optimize Enzymatic Preparation of Antibacterial Peptides from Tenebrio molitor Protein

doi:10.7506/spkx1002-6630-200915035

FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (15 ): 156-159.doi: 10.7506/spkx1002-6630-200915035

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Response Surface Methodology as An Approach to Optimize Enzymatic Preparation of Antibacterial Peptides from Tenebrio molitor Protein

LIU Han-ling1,2，PAN Yang-chang1,*，WANG Xiao-ying1，HU Li-feng2

(1. School of Chemistry and Chemical Engineering, Guangxi University, Nanning 530004, China；
2. Nanning Pangbo Biological Engineering Co. Ltd., Nanning 530004, China)

Received:2009-05-26 Online:2009-08-01 Published:2010-12-29
Contact: PAN Yang-chang1,*， E-mail:nnpyc0808@126.com

Abstract

Abstract:

Enzymolysis was applied to prepare antibacterial peptides from Tenebrio molitor protein. Tenebrio molitor protein was hydrolyzed with eight proteases respectively and among them trypsin was found to have the best comprehensive performance confirmed by the antibacterial activity and SDS pattern of corresponding hydrolysates as well as peptide concentration in their solution. The trypsin-catalyzed hydrolysis of Tenebrio molitor protein was optimized to attain the highest antibacterial activity using response surface design and a regression model for antibacterial activity as a function of substrate concentration, enzyme dose and hydrolysis duration were built up. Under optimized conditions: substrate concentration 11.84%, enzyme dose 4.05‰, pH 8.5 and temperature 40 ℃ for a hydrolysis duration of 5.86 h, the actual diameter of antibacterial circle of hydrolysates reached 16.54 mm, close to the predicted value of 16.98 mm.

Key words: antibacterial peptide, Tenebrio molitor, enzymolysis

CLC Number:

Q516

LIU Han-ling1,2，PAN Yang-chang1,*，WANG Xiao-ying1，HU Li-feng2. Response Surface Methodology as An Approach to Optimize Enzymatic Preparation of Antibacterial Peptides from Tenebrio molitor Protein[J]. FOOD SCIENCE, 2009, 30(15 ): 156-159.

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Response Surface Methodology as An Approach to Optimize Enzymatic Preparation of Antibacterial Peptides from Tenebrio molitor Protein

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