Lijun Zhang
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Lijun Zhang has a total of 16 co-authors. Here are the top co-authors by number of shared publications:
- Ao Zhang
Shenyang Agricultural University
1 shared publication - Chunlin Zhang
College of Life Science and Food Engineering, Inner Mongolia Minzu University, Tongliao 028000, China
1 shared publication - Daming Ren
Shenyang Agricultural University
1 shared publication - Fenglan Huang
College of Life Science and Food Engineering, Inner Mongolia Minzu University, Tongliao 028000, China
1 shared publication - Gang Wang
College of Life Science and Food Engineering, Inner Mongolia Minzu University, Tongliao 028000, China
1 shared publication - Guorui Li
College of Life Science and Food Engineering, Inner Mongolia University for the Nationalities, Tongliao 028000, China
1 shared publication
Latest Publications
- Open Access
- 21 December 2022
- Published by MDPI AG in Separations
- Vol. 10 (1) , 2
Identification and Functional Characterization of the RcFAH12 Promoter from Castor Bean in Arabidopsis thaliana
Castor (Ricinus communis L.) seed oil is the commercial source of ricinoleate, a valuable raw material used in many industries. Oleoyl-12-hydroxylase (RcFAH12) is a key enzyme in the biosynthesis of ricinoleate, accumulating nearly 90% of the triacylglycerol in castor seeds. Little is known about the transcriptional regulation of RcFAH12. We used rapid amplification of cDNA 5′ ends (5′RACE) to locate the transcription start site (TSS) of RcFAH12, and the sequence of a 2605 bp region, −2506~+99, surrounding the TSS was cloned. We then investigated these regions to promote β-glucuronidase (GUS) expression in transgenic Arabidopsis by the progressive 5′ and 3′ deletions strategies. The GUS staining showed that the GUS accumulation varied in tissues under the control of different deleted fragments of RcFAH12. In addition, the GUS expression driven by the RcFAH12 promoter markedly accumulated in transgenic seeds, which indicated that RcFAH12 might play an important role in the biosynthesis of ricinoleic acid. This study will lay a potential foundation for developing a tissue-specific promoter in oil-seed crops.
- 21 December 2022
- Published by MDPI AG in Separations
- Vol. 10 (1) , 2
Open AccessIdentification and Functional Characterization of the RcFAH12 Promoter from Castor Bean in Arabidopsis thaliana
Castor (Ricinus communis L.) seed oil is the commercial source of ricinoleate, a valuable raw material used in many industries. Oleoyl-12-hydroxylase (RcFAH12) is a key enzyme in the biosynthesis of ricinoleate, accumulating nearly 90% of the triacylglycerol in castor seeds. Little is known about the transcriptional regulation of RcFAH12. We used rapid amplification of cDNA 5′ ends (5′RACE) to locate the transcription start site (TSS) of RcFAH12, and the sequence of a 2605 bp region, −2506~+99, surrounding the TSS was cloned. We then investigated these regions to promote β-glucuronidase (GUS) expression in transgenic Arabidopsis by the progressive 5′ and 3′ deletions strategies. The GUS staining showed that the GUS accumulation varied in tissues under the control of different deleted fragments of RcFAH12. In addition, the GUS expression driven by the RcFAH12 promoter markedly accumulated in transgenic seeds, which indicated that RcFAH12 might play an important role in the biosynthesis of ricinoleic acid. This study will lay a potential foundation for developing a tissue-specific promoter in oil-seed crops.
- 26 June 2014
- Published by Springer Nature in Biotechnology Letters
- Vol. 36 (10) , 2103-2108
Introduction of two mutations into AroG increases phenylalanine production in Escherichia coli
L-Phenylalanine is an important amino acid commercially, and therefore optimization of its manufacture is of interest. We constructed a range of mutant alleles of AroG, the enzyme involved in the first step of phenylalanine biosynthesis. Three single-site mutant alleles were constructed (aroG8, aroG15, and aroG29), which were then combined to generate three double-site aroG fbr mutant alleles (aroG8/15, aroG8/29, and aroG15/29). Enzymatic activity, feedback inhibition, and fermentation were analyzed in all of the mutants. All double-site mutants, except AroG15/29, showed higher enzymatic activity and greater resistance to feedback inhibition than their respective single-site mutants. The E. coli strain carrying the aroG8/15 allele produced a phenylalanine titer of 26.78 g/l, a 116 % improvement over the control phenylalanine overproducing strain (12.41 g/l). Our findings provide an effective method for modifying phenylalanine biosynthetic genes, which may be applied to optimize the commercial manufacture of phenylalanine.
- 26 June 2014
- Published by Springer Nature in Biotechnology Letters
- Vol. 36 (10) , 2103-2108
Introduction of two mutations into AroG increases phenylalanine production in Escherichia coli
L-Phenylalanine is an important amino acid commercially, and therefore optimization of its manufacture is of interest. We constructed a range of mutant alleles of AroG, the enzyme involved in the first step of phenylalanine biosynthesis. Three single-site mutant alleles were constructed (aroG8, aroG15, and aroG29), which were then combined to generate three double-site aroG fbr mutant alleles (aroG8/15, aroG8/29, and aroG15/29). Enzymatic activity, feedback inhibition, and fermentation were analyzed in all of the mutants. All double-site mutants, except AroG15/29, showed higher enzymatic activity and greater resistance to feedback inhibition than their respective single-site mutants. The E. coli strain carrying the aroG8/15 allele produced a phenylalanine titer of 26.78 g/l, a 116 % improvement over the control phenylalanine overproducing strain (12.41 g/l). Our findings provide an effective method for modifying phenylalanine biosynthetic genes, which may be applied to optimize the commercial manufacture of phenylalanine.