Biochemical and molecular characterization of glucoamylase produced by the Aspergillus niger strain HPD-2

被引:0
作者
Perez-Rodriguez, Fernando [1 ,2 ]
Pliego-Arreaga, Raquel [3 ]
Silva-Martinez, Guillermo Antonio [1 ,4 ]
Cervantes-Montelongo, Juan Antonio [1 ,3 ]
机构
[1] Tecnol Nacl Mexico Celaya, Dept Ingn Bioquim & Ambiental, Guanajuato 38010, Mexico
[2] Univ Quetzalcoatl Irapuato, Dept Ciencias Biomed, Escuela Med, Guanajuato 36615, Mexico
[3] Univ Celaya, Escuela Med, Guanajuato 38080, Mexico
[4] Tecnol Nacl Mexico Celaya, Dept Ingn Bioquim & Ambiental, Tecnol Nacl Mexico, Catedras CONACYT, Guanajuato 38010, Mexico
来源
BIOTECNIA | 2024年 / 26卷 / 01期
关键词
Glucoamylase; A; niger; biochemical characteriza-tion; molecular characterization; enzyme kinetic; IMMOBILIZATION; EXPRESSION; SEQUENCE; GENE; CREA;
D O I
10.18633/biotecnia.v26i1.2024
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
Aspergillus niger HPD-2 has interesting growth characteris-tics, it grows at a temperature of 38 oC and pH of 3, it is also known to produce various enzymes of commercial interest such as glucoamylase, which is present in the medium even under non-inducible conditions and has important activity characteristics such as an optimum temperature of 70 oC and an optimum pH of 3-4. These features are very important be-cause they will help to minimize microbial contamination risk in industrial hydrolysis processes. For the characterization of A. niger HPD-2 glucoamylase, the presence and activity of the enzyme were verified in a non-inducing medium. The apparent kinetic parameters Km, Ki and Vmax were determined at 6.66 mM, 0.601 M and 66.5 mM/min, respectively, as well as its optimum pH and temperature activity (pH 3 and 70 degrees C). Comparatively speaking, these data are competitive against those reported for similar purified enzymes. On the other hand, DNA sequence analysis ofA. niger HPD-2 glucoamylase gene showed no changes in the promoter region or starch-binding domains. Therefore, the presence of the enzyme in a non-inducing medium could be related to changes in a repressor protein CreA.
引用
收藏
页码:5 / 15
页数:11
相关论文
共 41 条
[1]  
Abarca ML, 2000, REV IBEROAM MICOL, V17, pS79
[2]   Overexpression of amyA and glaA substantially increases glucoamylase activity in Aspergillus niger [J].
An, Xin ;
Ding, Chunjie ;
Zhang, Hui ;
Liu, Tianqi ;
Li, Jie .
ACTA BIOCHIMICA ET BIOPHYSICA SINICA, 2019, 51 (06) :638-644
[3]   A MATHEMATICAL MODEL FOR CONTINUOUS CULTURE OF MICROORGANISMS UTILIZING INHIBITORY SUBSTRATES [J].
ANDREWS, JF .
BIOTECHNOLOGY AND BIOENGINEERING, 1968, 10 (06) :707-+
[4]   Immobilization of glucoamylase onto spacer-arm attached magnetic poly(methylmethacrylate) microspheres: characterization and application to a continuous flow reactor [J].
Arica, MY ;
Yavuz, H ;
Patir, S ;
Denizli, A .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2000, 11 (2-3) :127-138
[5]   Performance of immobilized glucoamylase in a magnetically stabilized fluidized bed reactor (MSFBR) [J].
Bahar, T ;
Çelebi, SS .
ENZYME AND MICROBIAL TECHNOLOGY, 2000, 26 (01) :28-33
[6]   Aspergillus niger genomics: Past, present and into the future [J].
Baker, Scott E. .
MEDICAL MYCOLOGY, 2006, 44 :S17-S21
[7]  
Baltazar-Ramirez J., 1984, Tesis de licenciatura en ingenieria en biotecnologia
[8]  
Banerjee S, 2017, APPL FOOD BIOTECHNOL, V4, P19
[9]   Citric acid fromAspergillus niger: a comprehensive overview [J].
Behera, Bikash Chandra .
CRITICAL REVIEWS IN MICROBIOLOGY, 2020, 46 (06) :727-749
[10]  
Berka R M, 1992, Biotechnology, V23, P155