ReviewBioengineered
Recombinant bacterial amylopullulanases: developments and perspectives.
Review in Bioengineered. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 70 citations in OpenAlex.
- The crystal structure of GH57 family amylopullulanase reveals its dual binding pockets sharing the same catalytic dyad.Communications biology · 2025Article
- Long-read, multi-amplicon sequencing to explore genetic diversity associated with starch degrading phenotypes in amylolyticFrontiers in microbiology · 2025Article
- Molecular Cloning, Characterization, and Application of a Novel Multifunctional Isoamylase (MIsA) fromFoods (Basel, Switzerland) · 2024Article
- Glycogen availability and pH variation in a medium simulating vaginal fluid influence the growth of vaginal Lactobacillus species and Gardnerella vaginalis.BMC microbiology · 2023Article
- Characterization of a novel type of glycogen-degrading amylopullulanase from Lactobacillus crispatus.Applied microbiology and biotechnology · 2022Article
- Substrate Selectivity of a Novel Amylo-α-1,6-glucosidase fromFoods (Basel, Switzerland) · 2022Article
- Parallel N- and C-Terminal Truncations Facilitate Purification and Analysis of a 155-kDa Cold-Adapted Type-I Pullulanase.The protein journal · 2017Article
- Cohnella amylopullulanases: Biochemical characterization of two recombinant thermophilic enzymes.PloS one · 2017Article
- Structure and function of α-glucan debranching enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- Improving the Thermostability of Acidic Pullulanase from Bacillus naganoensis by Rational Design.PloS one · 2016Article
- Cold and Hot Extremozymes: Industrial Relevance and Current Trends.Frontiers in bioengineering and biotechnology · 2015Review
- Purification and characterization of a cold-adapted pullulanase from a psychrophilic bacterial isolate.Extremophiles : life under extreme conditions · 2014Article
- Novel maltotriose-hydrolyzing thermoacidophilic type III pullulan hydrolase from Thermococcus kodakarensis.Applied and environmental microbiology · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pullulanases are endo-acting enzymes capable of hydrolyzing α-1, 6-glycosidic linkages in starch, pullulan, amylopectin, and related oligosaccharides, while amylopullulanases are bifunctional enzymes with an active site capable of cleaving both α-1, 4 and α-1, 6 linkages in starch, amylose and other oligosaccharides, and α-1, 6 linkages in pullulan. The amylopullulanases are classified in GH13 and GH57 family enzymes based on the architecture of catalytic domain and number of conserved sequences. The enzymes with two active sites, one for the hydrolysis of α-1, 4- glycosidic bond and the other for α-1, 6-glycosidic bond, are called α-amylase-pullulanases, while amylopullulanases have only one active site for cleaving both α-1, 4- and α-1, 6-glycosidic bonds. The amylopullulanases produced by bacteria find applications in the starch and baking industries as a catalyst for one step starch liquefaction-saccharification for making various sugar syrups, as antistaling agent in bread and as a detergent additive.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.