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Molecules 2016, 21(1), 73; doi:10.3390/molecules21010073

High Milk-Clotting Activity Expressed by the Newly Isolated Paenibacillus spp. Strain BD3526

1
State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
2
State Key Laboratory of Dairy Biotechnology, Technology Center and Dairy Research Institute of Bright Dairy & Food Co. Ltd., Shanghai 200436, China
3
Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi 214122, China
4
Beijing Innovation Centre of Food Nutrition and Human Health, Beijing Technology & Business University, Beijing 100048, China
*
Author to whom correspondence should be addressed.
Academic Editor: Nancy D. Turner
Received: 16 October 2015 / Revised: 31 December 2015 / Accepted: 6 January 2016 / Published: 12 January 2016
(This article belongs to the Section Natural Products)
View Full-Text   |   Download PDF [1862 KB, uploaded 12 January 2016]   |  

Abstract

Paenibacillus spp. BD3526, a bacterium exhibiting a protein hydrolysis circle surrounded with an obvious precipitation zone on skim milk agar, was isolated from raw yak (Bos grunniens) milk collected in Tibet, China. Phylogenetic analysis based on 16S rRNA and whole genome sequence comparison indicated the isolate belong to the genus Paenibacillus. The strain BD3526 demonstrated strong ability to produce protease with milk clotting activity (MCA) in wheat bran broth. The protease with MCA was predominantly accumulated during the late-exponential phase of growth. The proteolytic activity (PA) of the BD3526 protease was 1.33-fold higher than that of the commercial R. miehei coagulant. A maximum MCA (6470 ± 281 SU mL−1) of the strain BD3526 was reached under optimal cultivation conditions. The protease with MCA was precipitated from the cultivated supernatant of wheat bran broth with ammonium sulfate and purified by anion-exchange chromatography. The molecular weight of the protease with MCA was determined as 35 kDa by sodium dodecyl sulfate-polyacrylamide gels electrophoresis (SDS-PAGE) and gelatin zymography. The cleavage site of the BD3526 protease with MCA in κ-casein was located at the Met106–Ala107 bond, as determined by mass spectrometry analysis. View Full-Text
Keywords: Paenibacillus; coagulant; milk clotting activity; proteolytic activity Paenibacillus; coagulant; milk clotting activity; proteolytic activity
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MDPI and ACS Style

Hang, F.; Liu, P.; Wang, Q.; Han, J.; Wu, Z.; Gao, C.; Liu, Z.; Zhang, H.; Chen, W. High Milk-Clotting Activity Expressed by the Newly Isolated Paenibacillus spp. Strain BD3526. Molecules 2016, 21, 73.

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