Ruomin Li
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Ruomin Li has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
- Chengzhong Li
School of Food and Health
1 shared publication - Huanxin Zhang
School of Food Science and Technology, Jiangsu Agri-animal Husbandry Vocational College, 8 Fenghuang East Road, Taizhou 225300, China
1 shared publication - Huanxin Zhang
College of Geography and Environment, Shandong Normal University, Jinan 250014, China
1 shared publication - Jingjing Ye
Trauma Medicine Centre Peking University People's Hospital, Key Laboratory of Trauma and Neural Regeneration (Peking University), Ministry of Education, National Centre for Trauma Medicine , Beijing
1 shared publication Mengwei Zhu
School of Food Science and Technology, Jiangsu Agri-animal Husbandry Vocational College, Taizhou 225300, People’s Republic of China
1 shared publicationSaikun Pan
College of Food Science and Engineering, Jiangsu Ocean University, Lianyungang 222005, People’s Republic of China
1 shared publication
Latest Publications
- Open Access
- 26 September 2022
- Published by American Chemical Society (ACS) in ACS Omega
- Vol. 7 (39) , 34801-34809
Proteomic Analysis of the Inflorescence Stem Mechanical Strength Difference in Herbaceous Peonies (Paeonia lactiflora Pall.)
The herbaceous peony (Paeonia lactiflora Pall.) is a traditional rare flower in China, and production of its cut flowers has developed gradually in many places of the world. However, the inflorescence stems of some P. lactiflora cultivars have such low mechanical strength that the cut flower production was severely restricted. To better understand the causes of this problem from a protein expression level, two P. lactiflora cultivars with different inflorescence stem mechanical strengths were analyzed by two-dimensional electrophoresis and MALDI-TOF/MS. More than 1700 clear protein spots were detected, 53 of which varied significantly. Moreover, 23 of the differentially expressed proteins were identified and confirmed and are involved in various biological processes such as metabolism, protein biosynthesis and transport, signal transduction, and defensive response. Especially, cinnamyl alcohol dehydrogenase (CAD) and xyloglucan endotransglucosylase/hydrolase (XTH) were strongly connected to the inflorescence stem mechanical strength in P. lactiflora.
- 26 September 2022
- Published by American Chemical Society (ACS) in ACS Omega
- Vol. 7 (39) , 34801-34809
Open AccessProteomic Analysis of the Inflorescence Stem Mechanical Strength Difference in Herbaceous Peonies (Paeonia lactiflora Pall.)
The herbaceous peony (Paeonia lactiflora Pall.) is a traditional rare flower in China, and production of its cut flowers has developed gradually in many places of the world. However, the inflorescence stems of some P. lactiflora cultivars have such low mechanical strength that the cut flower production was severely restricted. To better understand the causes of this problem from a protein expression level, two P. lactiflora cultivars with different inflorescence stem mechanical strengths were analyzed by two-dimensional electrophoresis and MALDI-TOF/MS. More than 1700 clear protein spots were detected, 53 of which varied significantly. Moreover, 23 of the differentially expressed proteins were identified and confirmed and are involved in various biological processes such as metabolism, protein biosynthesis and transport, signal transduction, and defensive response. Especially, cinnamyl alcohol dehydrogenase (CAD) and xyloglucan endotransglucosylase/hydrolase (XTH) were strongly connected to the inflorescence stem mechanical strength in P. lactiflora.
- Open Access
- 19 May 2022
- Published by American Chemical Society (ACS) in ACS Omega
- Vol. 7 (21) , 17632-17640
Preparation of Slowly Digested Corn Starch Using Branching Enzyme and Immobilized α-Amylase
The aim of this study was to modify the digestibility and structure of corn starch by treatment with compound enzymes. Corn starch was treated with two enzymes (α-amylase, which catalyzes hydrolysis, and branching enzyme, a transglycosidase that catalyzes branch formation), and the reaction was monitored by determining the content of slowly digestible starch in the reaction product. The fine structure and physical and chemical properties of enzyme-modified starch samples were analyzed using scanning electron microscopy, gel chromatography, and X-ray diffraction methods; modified starch has a high degree of branching, a high proportion of short-chain branched structures, and greatly improved solubility. The results show that the slow digestion performance of corn starch was significantly improved after hydrolysis by α-amylase for 4 h and treatment with branching enzyme for 6 h. These results show that enzymatic modification of corn starch can improve its slow digestibility properties.
- 19 May 2022
- Published by American Chemical Society (ACS) in ACS Omega
- Vol. 7 (21) , 17632-17640
Open AccessPreparation of Slowly Digested Corn Starch Using Branching Enzyme and Immobilized α-Amylase
The aim of this study was to modify the digestibility and structure of corn starch by treatment with compound enzymes. Corn starch was treated with two enzymes (α-amylase, which catalyzes hydrolysis, and branching enzyme, a transglycosidase that catalyzes branch formation), and the reaction was monitored by determining the content of slowly digestible starch in the reaction product. The fine structure and physical and chemical properties of enzyme-modified starch samples were analyzed using scanning electron microscopy, gel chromatography, and X-ray diffraction methods; modified starch has a high degree of branching, a high proportion of short-chain branched structures, and greatly improved solubility. The results show that the slow digestion performance of corn starch was significantly improved after hydrolysis by α-amylase for 4 h and treatment with branching enzyme for 6 h. These results show that enzymatic modification of corn starch can improve its slow digestibility properties.