It appears you don't have support to open PDFs in this web browser. To view this file, Open with your PDF reader
Abstract
In the development of symbiotic sourdough starters, it is necessary to examine the enzymatic profile of all potential lactic acid bacteria (LAB) strains. The enzymatic profile of 3 strains of the genus Lactiplantibacillus and 2 strains of the genus Levilactobacillus was investigated using the API ZYM system (Biomerieux®, France) and in separate experiments the amylolytic and proteolytic activity were determined by the agar-diffusion method with wells. All Lactiplantibacillus strains possessed: leucine arylamidase, valine arylamidase, cysteine arylamidase, acid phosphatase, phosphohydrolase, β-galactosidase, α- glucosidase, β-glucosidase and α-glucosaminidase. The two Levilactobacillus brevis strains possessed: lipase C4, esterase lipase C8, leucine arylamidase, valine arylamidase, cysteine arylamidase, acid phosphatase, naphthol-AS-BI-phosphohydrolase, α-galactosidase, β-galactosidase, α-glucosidase, β- glucosidase. Lactiplantibacillus plantarum L1 demonstrated the highest amylolytic activity, and Levilactobacillus brevis X4 has the lowest. Lactiplantibacillus plantarum L1 exhibited the highest proteolytic activity, and Levilactobacillus brevis X4 - the lowest. The proteolysis was due to the production of inducible proteolytic enzymes by the LAB cells, as well as acid hydrolysis resulting from the lactic, acetic and other organic acids produced by the strains. The five LAB strains possess a rich and diverse enzyme profile, which is a prerequisite for their application in the development of symbiotic starters for sourdough bread.
You have requested "on-the-fly" machine translation of selected content from our databases. This functionality is provided solely for your convenience and is in no way intended to replace human translation. Show full disclaimer
Neither ProQuest nor its licensors make any representations or warranties with respect to the translations. The translations are automatically generated "AS IS" and "AS AVAILABLE" and are not retained in our systems. PROQUEST AND ITS LICENSORS SPECIFICALLY DISCLAIM ANY AND ALL EXPRESS OR IMPLIED WARRANTIES, INCLUDING WITHOUT LIMITATION, ANY WARRANTIES FOR AVAILABILITY, ACCURACY, TIMELINESS, COMPLETENESS, NON-INFRINGMENT, MERCHANTABILITY OR FITNESS FOR A PARTICULAR PURPOSE. Your use of the translations is subject to all use restrictions contained in your Electronic Products License Agreement and by using the translation functionality you agree to forgo any and all claims against ProQuest or its licensors for your use of the translation functionality and any output derived there from. Hide full disclaimer