A highly stable raw starch digesting ?-amylase from Nile tilapia (Oreochromis niloticus) viscera

被引:5
作者
Ferreira, Amalia [1 ]
Cahu, Thiago [1 ]
Xu, Jinchuan [2 ,3 ]
Blennow, Andreas [2 ]
Bezerra, Ranilson [1 ]
机构
[1] Univ Fed Pernambuco, Dept Biochem, Lab Enzymol LABENZ, Recife, PE, Brazil
[2] Univ Copenhagen, Fac Sci, Dept Plant & Environm Sci, Copenhagen, Denmark
[3] South China Univ Technol, Sch Food Sci & Engn, Guangzhou, Peoples R China
关键词
Starch; Amylase; Digestive enzymes; Fish processing waste; Starch hydrolysis; ALPHA-AMYLASE; BIOCHEMICAL-CHARACTERIZATION; PURIFICATION; HYDROLYSIS; CLONING; RESISTANT; BACTERIUM; STRAIN; ENZYME; GENE;
D O I
10.1016/j.foodchem.2021.129513
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
A raw starch digesting ?-amylase from Nile tilapia (Oreochromis niloticus) intestine was identified. The ?-amylase, AMY-T, had an estimated molecular weight of 60 kDa and purified to near homogeneity. AMY-T showed an apparent KM 4.78 mg/mL and Vmax 0.44 mg/mL/min) towards soluble starch. It was highly stable for 24 h in the pH range 3.0?10.0, and to solvents like methanol, isopropanol, butanol, dimethylformamide, DMSO and ethylether. AMY-T was able to digest different carbohydrates, mainly showing endo-activity. Importantly, AMY-T was catalytically efficient and adsorbing towards raw potato starch at temperature documented for other raw starch digesting ?-amylases. Thin layer and anion exchange chromatography characterization showed that the end products of raw starch hydrolysis were glucose, maltose and maltodextrins, with degree of polymerisation ranging 1?8. Scanning electron microscopy analysis of the AMY-T treated starch granules documented both granular exo- and endo-attack by AMY-T. These catalytic capabilities suggest high potential for AMY-T for industrial use.
引用
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页数:10
相关论文
共 41 条
[1]   Contributing to fisheries sustainability by making the best possible use of their resources: the BEFAIR initiative [J].
Alonso, Antonio A. ;
Antelo, Luis T. ;
Otero-Muras, Irene ;
Perez-Galvez, Raul .
TRENDS IN FOOD SCIENCE & TECHNOLOGY, 2010, 21 (11) :569-578
[2]   Molecular cloning and biochemical characterization of a thermoacidophilic, organic-solvent tolerant α-amylase from a Bacillus strain in Escherichia coli [J].
Asoodeh, Ahmad ;
Emtenani, Shamsi ;
Emtenani, Shirin ;
Jalal, Razieh ;
Housaindokht, Mohammad Reza .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2014, 99 :114-120
[3]   AMYLASES, ALPHA AND BETA [J].
BERNFELD, P .
METHODS IN ENZYMOLOGY, 1955, 1 :149-158
[4]   Partial purification and characterization of a thermostable trypsin from pyloric caeca of tambaqui (Colossoma macropomum) [J].
Bezerra, RS ;
Santos, JF ;
Paiva, PMG ;
Correia, MTS ;
Coelho, LCBB ;
Vieira, VLA ;
Carvalho, LB .
JOURNAL OF FOOD BIOCHEMISTRY, 2001, 25 (03) :199-210
[5]   The degree of starch phosphorylation is related to the chain length distribution of the neutral and the phosphorylated chains of amylopectin [J].
Blennow, A ;
Bay-Smidt, AM ;
Wischmann, B ;
Olsen, CE ;
Moller, BL .
CARBOHYDRATE RESEARCH, 1998, 307 (1-2) :45-54
[6]  
Bozic N., 2017, Amylase, V1, P12, DOI [10.1515/amylase-2017-0002, DOI 10.1515/AMYLASE-2017-0002]
[7]   First Principles Insight into the α-Glucan Structures of Starch: Their Synthesis, Conformation, and Hydration [J].
Damager, Iben ;
Engelsen, Soren Balling ;
Blennow, Andreas ;
Moller, Birger Lindberg ;
Motawia, Mohammed Saddik .
CHEMICAL REVIEWS, 2010, 110 (04) :2049-2080
[8]   Characterisation of three starch degrading enzymes: Thermostable β-amylase, maltotetraogenic and maltogenic α-amylases [J].
Derde, L. J. ;
Gomand, S. V. ;
Courtin, C. M. ;
Delcour, J. A. .
FOOD CHEMISTRY, 2012, 135 (02) :713-721
[9]   Mechanisms of starch digestion by α-amylase-Structural basis for kinetic properties [J].
Dhital, Sushil ;
Warren, Frederick J. ;
Butterworth, Peter J. ;
Ellis, Peter R. ;
Gidley, Michael J. .
CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION, 2017, 57 (05) :875-892
[10]   Purification, Sequencing, and Biochemical Characterization of a Novel Calcium-Independent α-Amylase AmyTVE from Thermoactinomyces vulgaris [J].
El-Sayed, Ahmed K. A. ;
Abou Dobara, Mohamed I. ;
El-Fallal, Amira A. ;
Omar, Noha F. .
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2013, 170 (03) :483-497