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Catalysts 2018, 8(8), 325; https://doi.org/10.3390/catal8080325

Study of Extraction and Enzymatic Properties of Cell-Envelope Proteinases from a Novel Wild Lactobacillus plantarum LP69

1
,
1,* , 2
,
3,* , 1
and
1
1
School of Food and Biological Engineering, Shaanxi University of Science and Technology, Xi’an 710021, China
2
College of Animal Science and Technology, Northwest A&F University, Yangling 712100, China
3
College of Food Engineering and Nutritional Science, Shaanxi Normal University, Xi’an 710119, China
*
Authors to whom correspondence should be addressed.
Received: 17 July 2018 / Revised: 5 August 2018 / Accepted: 7 August 2018 / Published: 8 August 2018
(This article belongs to the Special Issue Biocatalysts: Design and Application)
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Abstract

Lactobacilli cell-envelope proteinases (CEPs) have been widely used in the development of new streams of blockbuster nutraceuticals because of numerous biopharmaceutical potentials; thus, the development of viable methods for CEP extraction and the improvement of extraction efficiency will promote their full-scale application. In this study, CEP from a novel wild Lactobacillus plantarum LP69 was released from cells by incubating in calcium-free buffer. The extraction conditions of CEP were optimized by response surface methodology with the enzyme activity and specific activity as the detective marker. The optimal extraction conditions were: time of 80 min, temperature of 39 °C and buffer pH of 6.5. Under these conditions, enzyme activity and specific activity were (23.94 ± 0.86) U/mL and (1.37 ± 0.03) U/mg, respectively, which were well matched with the predicted values (22.12 U/mL and 1.36 U/mg). Optimal activity of the crude CEP occurred at pH 8.0 and 40 °C. It is a metallopeptidase, activated by Ca2+, inhibited by Zn2+ and ethylene-diamine-tetra-acetic acid, and a serine proteinase which is inhibited by phenylmethylsulfonyl fluoride. Kinetic studies showed that CEP from LP69 could hydrolyze whey protein, lactoglobulin and casein. Our study improves the extraction efficiency of CEPs from LP69, providing the reference for their industrial development. View Full-Text
Keywords: Lactobacillus plantarum LP69; cell-envelope proteinases; extraction conditions; response surface methodology; enzymatic properties Lactobacillus plantarum LP69; cell-envelope proteinases; extraction conditions; response surface methodology; enzymatic properties
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Chen, H.; Huang, J.; Cao, B.; Chen, L.; Song, N.; Lei, N. Study of Extraction and Enzymatic Properties of Cell-Envelope Proteinases from a Novel Wild Lactobacillus plantarum LP69. Catalysts 2018, 8, 325.

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