Bacterial 1,4-α-glucan branching enzymes: characteristics, preparation and commercial applications

被引:32
作者
Ban, Xiaofeng [1 ]
Dhoble, Abhishek S. [2 ]
Li, Caiming [1 ]
Gu, Zhengbiao [1 ,3 ,4 ]
Hong, Yan [1 ]
Cheng, Li [1 ]
Holler, Tod P. [5 ]
Kaustubh, Bhalerao [2 ]
Li, Zhaofeng [1 ,3 ,4 ]
机构
[1] Jiangnan Univ, Sch Food Sci & Technol, Wuxi 21422, Jiangsu, Peoples R China
[2] Univ Illinois, Dept Agr & Biol Engn, Urbana, IL USA
[3] Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi, Jiangsu, Peoples R China
[4] Jiangnan Univ, Collaborat Innovat Ctr Safety & Qual Control, Wuxi, Jiangsu, Peoples R China
[5] Univ Michigan, Dept Med Chem, Ann Arbor, MI 48109 USA
基金
中国国家自然科学基金; 中国博士后科学基金;
关键词
14-alpha-glucan branching enzymes; bacterial GBEs; identification; action pattern; structure; industrial applications; ALPHA-AMYLASE FAMILY; ESCHERICHIA-COLI; BACILLUS-STEAROTHERMOPHILUS; STRUCTURAL SIMILARITY; CRYSTAL-STRUCTURES; MOLECULAR-CLONING; GLYCOGEN; STARCH; GENE; AMYLOPECTIN;
D O I
10.1080/07388551.2020.1713720
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The 1,4-alpha-glucan branching enzymes (GBEs) are ubiquitously distributed in animals, microorganisms and plants. These enzymes modify the structure of both starch and glycogen; changing the frequency and position of branches by forming new alpha-1,6-glucosidic linkages. In organisms, controlling the number and distribution of branches is an irreplaceable process that maintains the physiological state of starch and glycogen in the cell. The process is also the foundation for the industrial applications of GBEs. So far, a number of GBEs have been identified in eukaryotes and prokaryotes as researchers searched for GBEs with optimal properties. Among them, bacterial GBEs have received particular attention due to the convenience of heterologous expression and industrial applications of GBEs from bacteria than GBEs from other sources. The advantages of bacterial GBEs in potential applications stimulated the investigations of bacterial GBEs in terms of their structure and properties. However, full exploitation of GBEs in commercial applications is still in its infancy because of the disadvantages of currently available enzymes and of limited imagination with respect to future possibilities. Thus, in this review, we present an overview of the bacterial GBEs including their structure, biochemical properties and commercial applications in order to depict the whole picture of bacterial GBEs.
引用
收藏
页码:380 / 396
页数:17
相关论文
共 81 条
[1]   The X-ray crystallographic structure of Escherichia coli branching enzyme [J].
Abad, MC ;
Binderup, K ;
Rios-Steiner, J ;
Arni, RK ;
Preiss, J ;
Geiger, JH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (44) :42164-42170
[2]   From bacterial glycogen to starch: Understanding the biogenesis of the plant starch granule [J].
Ball, SG ;
Morell, MK .
ANNUAL REVIEW OF PLANT BIOLOGY, 2003, 54 :207-233
[3]   Thermostabilization of a thermophilic 1,4-α-glucan branching enzyme through C-terminal truncation [J].
Ban, Xiaofeng ;
Liu, Yiting ;
Zhang, Yuzhu ;
Gu, Zhengbiao ;
Li, Caiming ;
Cheng, Li ;
Hong, Yan ;
Dhoble, Abhishek S. ;
Li, Zhaofeng .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2018, 107 :1510-1518
[4]   Glutamate-459 is important for Escherichia coli branching enzyme activity [J].
Binderup, K ;
Preiss, J .
BIOCHEMISTRY, 1998, 37 (25) :9033-9037
[5]   Limited proteolysis of branching enzyme from Escherichia coli [J].
Binderup, K ;
Mikkelsen, R ;
Preiss, J .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2000, 377 (02) :366-371
[6]   Two potentially novel amylolytic enzyme specificities in the prokaryotic glycoside hydrolase a-amylase family GH57 [J].
Blesak, Karol ;
Janecek, Stefan .
MICROBIOLOGY-SGM, 2013, 159 :2584-2593
[7]   Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57 [J].
Blesak, Karol ;
Janecek, Stefan .
EXTREMOPHILES, 2012, 16 (03) :497-506
[8]   TISSUE-SPECIFIC GLYCOGEN BRANCHING ISOENZYMES IN A MULTICELLULAR PROKARYOTE, STREPTOMYCES-COELICOLOR A3(2) [J].
BRUTON, CJ ;
PLASKITT, KA ;
CHATER, KF .
MOLECULAR MICROBIOLOGY, 1995, 18 (01) :89-99
[9]   Molecular cloning, functional expression and purification of a glucan branching enzyme from Neisseria denitrificans [J].
Büttcher, V ;
Quanz, M ;
Willmitzer, L .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1999, 1432 (02) :406-412
[10]   The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics [J].
Cantarel, Brandi L. ;
Coutinho, Pedro M. ;
Rancurel, Corinne ;
Bernard, Thomas ;
Lombard, Vincent ;
Henrissat, Bernard .
NUCLEIC ACIDS RESEARCH, 2009, 37 :D233-D238