Literature DB >> 33715051

Aspects and Recent Trends in Microbial α-Amylase: a Review.

Jai Shankar Paul1, Nisha Gupta1, Esmil Beliya1,2, Shubhra Tiwari1, Shailesh Kumar Jadhav3.   

Abstract

α-Amylases are the oldest and versatile starch hydrolysing enzymes which can replace chemical hydrolysis of starch in industries. It cleaves the α-(1,4)-D-glucosidic linkage of starch and other related polysaccharides to yield simple sugars like glucose, maltose and limit dextrin. α-Amylase covers about 30% shares of the total enzyme market. On account of their superior features, α-amylase is the most widely used among all the existing amylases for hydrolysis of polysaccharides. Endo-acting α-amylase of glycoside hydrolase family 13 is an extensively used biocatalyst and has various biotechnological applications like in starch processing, detergent, textile, paper and pharmaceutical industries. Apart from these, it has some novel applications including polymeric material for drug delivery, bioremediating agent, biodemulsifier and biofilm inhibitor. The present review will accomplish the research gap by providing the unexplored aspects of microbial α-amylase. It will allow the readers to know about the works that have already been done and the latest trends in this field. The manuscript has covered the latest immobilization techniques and the site-directed mutagenesis approaches which are readily being performed to confer the desirable property in wild-type α-amylases. Furthermore, it will state the inadequacies and the numerous obstacles coming in the way of its production during upstream and downstream steps and will also suggest some measures to obtain stable and industrial-grade α-amylase.
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Biocatalyst; Drug delivery; Glycoside hydrolases; Glycosidic linkage; α-Amylase

Year:  2021        PMID: 33715051     DOI: 10.1007/s12010-021-03546-4

Source DB:  PubMed          Journal:  Appl Biochem Biotechnol        ISSN: 0273-2289            Impact factor:   2.926


  90 in total

1.  Identification and phylogenetic characterization of a new subfamily of α-amylase enzymes from marine microorganisms.

Authors:  Yang Liu; Yin Lei; Xuecheng Zhang; Yi Gao; Yazhong Xiao; Hui Peng
Journal:  Mar Biotechnol (NY)       Date:  2011-11-11       Impact factor: 3.619

2.  Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of alpha-amylase-related proteins.

Authors:  Mark R Stam; Etienne G J Danchin; Corinne Rancurel; Pedro M Coutinho; Bernard Henrissat
Journal:  Protein Eng Des Sel       Date:  2006-11-02       Impact factor: 1.650

Review 3.  α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.

Authors:  Štefan Janeček; Birte Svensson; E Ann MacGregor
Journal:  Cell Mol Life Sci       Date:  2013-06-27       Impact factor: 9.261

4.  Production, characterization and application of thermostable, alkaline α-amylase (AA11) from Bacillus cereus strain SP-CH11 isolated from Chilika Lake.

Authors:  Sonali Priyadarshini; Sukanta Kumar Pradhan; Pratima Ray
Journal:  Int J Biol Macromol       Date:  2019-11-20       Impact factor: 6.953

5.  A novel high maltose-forming α-amylase from Rhizomucor miehei and its application in the food industry.

Authors:  Yu-Chuan Wang; Hui-Fang Hu; Jun-Wen Ma; Qiao-Juan Yan; Hai-Jie Liu; Zheng-Qiang Jiang
Journal:  Food Chem       Date:  2019-08-30       Impact factor: 7.514

6.  Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose.

Authors:  Z Fujimoto; K Takase; N Doui; M Momma; T Matsumoto; H Mizuno
Journal:  J Mol Biol       Date:  1998-03-27       Impact factor: 5.469

7.  Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution.

Authors:  M Machius; G Wiegand; R Huber
Journal:  J Mol Biol       Date:  1995-03-03       Impact factor: 5.469

8.  Production and properties of a raw-starch-degrading amylase from the thermophilic and alkaliphilic Bacillus sp. TS-23.

Authors:  L L Lin; C C Chyau; W H Hsu
Journal:  Biotechnol Appl Biochem       Date:  1998-08       Impact factor: 2.431

9.  Horizontal gene transfer from Eukarya to bacteria and domain shuffling: the alpha-amylase model.

Authors:  J-L Da Lage; G Feller; S Janecek
Journal:  Cell Mol Life Sci       Date:  2004-01       Impact factor: 9.261

10.  Production of a novel α-amylase by Bacillus atrophaeus NRC1 isolated from honey: Purification and characterization.

Authors:  Ahmed M Abd-Elaziz; Eman A Karam; Manal M Ghanem; Maysa E Moharam; Amany L Kansoh
Journal:  Int J Biol Macromol       Date:  2020-01-13       Impact factor: 6.953

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Journal:  Foods       Date:  2022-06-21

2.  Production of extracellular α-amylase by single-stage steady-state continuous cultures of Candida wangnamkhiaoensis in an airlift bioreactor.

Authors:  Griselda Ma Chávez-Camarillo; Perla Vianey Lopez-Nuñez; Raziel Arturo Jiménez-Nava; Erick Aranda-García; Eliseo Cristiani-Urbina
Journal:  PLoS One       Date:  2022-03-01       Impact factor: 3.240

3.  Pudding Proteomics: Cyclomaltodextrin Glucanotransferase and Microbial Proteases Can Liquefy Extended Shelf Life Dairy Products.

Authors:  Kristina J H Kleinwort; Maria Weigand; Lydia Hoffmann; Roxane L Degroote; Richard Dietrich; Erwin Märtlbauer; Stefanie M Hauck; Cornelia A Deeg
Journal:  Metabolites       Date:  2022-03-17
  3 in total

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