PMID- 23525937
OWN - NLM
STAT- MEDLINE
DCOM- 20131021
LR  - 20130508
IS  - 1432-0614 (Electronic)
IS  - 0175-7598 (Linking)
VI  - 97
IP  - 10
DP  - 2013 May
TI  - An overview on alcohol oxidases and their potential applications.
PG  - 4259-75
LID - 10.1007/s00253-013-4842-9 [doi]
AB  - Alcohol oxidases (Alcohol: O(2) Oxidoreductase; EC 1.1.3.x) are flavoenzymes that 
      catalyze the oxidation of alcohols to the corresponding carbonyl compounds with a 
      concomitant release of hydrogen peroxide. Based on substrate specificity, alcohol 
      oxidases may be categorized broadly into four different groups namely, (a) short 
      chain alcohol oxidase (SCAO), (b) long chain alcohol oxidase (LCAO), (c) aromatic 
      alcohol oxidase (AAO), and (d) secondary alcohol oxidase (SAO). The sources 
      reported for these enzymes are mostly limited to bacteria, yeast, fungi, plant, 
      insect, and mollusks. However, the quantum of reports for each category of 
      enzymes considerably varies across these sources. The enzymes belonging to SCAO 
      and LCAO are intracellular in nature, whereas AAO and SAO are mostly secreted to 
      the medium. SCAO and LCAO are invariably reported as multimeric proteins with 
      very high holoenzyme molecular masses, but the molecular characteristics of these 
      enzymes are yet to be clearly elucidated. One of the striking features of the 
      alcohol oxidases that make them distinct from the widely known alcohol 
      dehydrogenase is the avidly bound cofactor to the redox center of these enzymes 
      that obviate the need to supplement cofactor during the catalytic reaction. These 
      flavin-based redox enzymes have gained enormous importance in the development of 
      various industrial processes and products primarily for developing biosensors and 
      production of various industrially useful carbonyl compounds. The present review 
      provides an overview on alcohol oxidases from different categories focusing 
      research on these oxidases during the last decade along with their potential 
      industrial applications.
FAU - Goswami, Pranab
AU  - Goswami P
AD  - Department of Biotechnology, Indian Institute of Technology Guwahati, Guwahati, 
      781 039 Assam, India. pgoswami@iitg.ernet.in
FAU - Chinnadayyala, Soma Sekhar R
AU  - Chinnadayyala SS
FAU - Chakraborty, Mitun
AU  - Chakraborty M
FAU - Kumar, Adepu Kiran
AU  - Kumar AK
FAU - Kakoti, Ankana
AU  - Kakoti A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20130326
PL  - Germany
TA  - Appl Microbiol Biotechnol
JT  - Applied microbiology and biotechnology
JID - 8406612
RN  - 0 (Alcohols)
RN  - EC 1.1.- (Alcohol Oxidoreductases)
RN  - EC 1.1.3.13 (alcohol oxidase)
SB  - IM
MH  - Alcohol Oxidoreductases/chemistry/*metabolism
MH  - Alcohols/metabolism
MH  - Animals
MH  - Catalysis
MH  - Microbiology
MH  - Models, Molecular
MH  - Substrate Specificity
EDAT- 2013/03/26 06:00
MHDA- 2013/10/22 06:00
CRDT- 2013/03/26 06:00
PHST- 2012/12/07 00:00 [received]
PHST- 2013/03/07 00:00 [accepted]
PHST- 2013/03/06 00:00 [revised]
PHST- 2013/03/26 06:00 [entrez]
PHST- 2013/03/26 06:00 [pubmed]
PHST- 2013/10/22 06:00 [medline]
AID - 10.1007/s00253-013-4842-9 [doi]
PST - ppublish
SO  - Appl Microbiol Biotechnol. 2013 May;97(10):4259-75. doi: 
      10.1007/s00253-013-4842-9. Epub 2013 Mar 26.