Li Li
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Li Li has a total of 5 co-authors. Here are the top co-authors by number of shared publications:
- Gongliang Liu
College of Light Industry and Food Sciences, Guangdong Key Laboratory of Science and Technology of Lingnan Special Food, Zhongkai University of Agriculture and Engineering, Guangzhou, China
1 shared publication Jinglong Liang
Affiliation College of Light Industry and Food Science, Zhongkai University of Agriculture and Engineering, Guangzhou, China
1 shared publicationWenJuan Jiao
Affiliation Guangdong Academy of Agricultural Sciences, Sericultural & Agri-Food Research Institute, Guangzhou, China
1 shared publicationYing Wang
Affiliation College of Light Industry and Food Science, Zhongkai University of Agriculture and Engineering, Guangzhou, China
1 shared publicationYongtao Fei
Affiliation College of Light Industry and Food Science, Zhongkai University of Agriculture and Engineering, Guangzhou, China
1 shared publication
Latest Publications
- Open Access
- 17 July 2020
- Published by Public Library of Science (PLoS) in PLOS ONE
- Vol. 15 (7) , e0235687
Cloning and expression of a novel α-galactosidase from Lactobacillus amylolyticus L6 with hydrolytic and transgalactosyl properties
Lactobacillus amylolyticus L6, a gram-positive amylolytic bacterium isolated from naturally fermented tofu whey (NFTW), was able to hydrolyze raffinose and stachyose for the production of α-galactosidase. The cell-free extract of L. amylolyticus L6 was found to exhibit glycosyltransferase activity to synthesize α-galacto-oligosaccharides (GOS) with melibiose as substrate. The coding genes of α-galactosidase were identified in the genome of L. amylolyticus L6. The α-galactosidase (AglB) was placed into GH36 family by amino acid sequence alignments with other α-galactosidases from lactobacilli. The optimal reaction conditions of pH and temperature for AglB were pH 6.0 and 37°C, respectively. Besides, potassium ion was found to improve the activity of AglB while divalent mercury ion, copper ion and zinc ion displayed different degrees of inhibition effect. Under the optimum reaction condition, AglB could catalyze the synthesis of GOS with degree of polymerization (DP) ≥5 by using 300 mM melibiose concentration as substrate. The maximum yield of GOS with (DP) ≥3 could reach 31.56% (w/w). Transgalactosyl properties made AglB a potential candidate for application in the production of GOS.
- 17 July 2020
- Published by Public Library of Science (PLoS) in PLOS ONE
- Vol. 15 (7) , e0235687
Open AccessCloning and expression of a novel α-galactosidase from Lactobacillus amylolyticus L6 with hydrolytic and transgalactosyl properties
Lactobacillus amylolyticus L6, a gram-positive amylolytic bacterium isolated from naturally fermented tofu whey (NFTW), was able to hydrolyze raffinose and stachyose for the production of α-galactosidase. The cell-free extract of L. amylolyticus L6 was found to exhibit glycosyltransferase activity to synthesize α-galacto-oligosaccharides (GOS) with melibiose as substrate. The coding genes of α-galactosidase were identified in the genome of L. amylolyticus L6. The α-galactosidase (AglB) was placed into GH36 family by amino acid sequence alignments with other α-galactosidases from lactobacilli. The optimal reaction conditions of pH and temperature for AglB were pH 6.0 and 37°C, respectively. Besides, potassium ion was found to improve the activity of AglB while divalent mercury ion, copper ion and zinc ion displayed different degrees of inhibition effect. Under the optimum reaction condition, AglB could catalyze the synthesis of GOS with degree of polymerization (DP) ≥5 by using 300 mM melibiose concentration as substrate. The maximum yield of GOS with (DP) ≥3 could reach 31.56% (w/w). Transgalactosyl properties made AglB a potential candidate for application in the production of GOS.