SGNH hydrolase-type esterase domain containing Cbes-AcXE2: a novel and thermostable acetyl xylan esterase from Caldicellulosiruptor bescii

Soni, Surabhi; Sathe, Sneha S.; Odaneth, Annamma A.; Lali, Arvind; Chandrayan, Sanjeev K.

doi:10.1007/s00792-017-0934-2

Cited by 14 publications

(14 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Additionally, very little activity was observed for the long-chain substrates p-NDe (C 10 ), p-NDo (C 12 ), or p-nitrophenyl phosphate (p-NPP). This preference for short-chain p-NP esters was also observed for other SGNH-type family members like Cbes-AcXE2 [24] or EstL5 [25]. However, Ser 29 mutation abolished most of the hydrolytic activity for p-NP esters.…”

Section: Characterizations Of Hasgnh1supporting

confidence: 66%

Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus

Yoo

Jeon

et al. 2020

Biotechnol Biofuels

View full text Add to dashboard Cite

Background: Biodiesel and flavor compound production using enzymatic transesterification by microbial lipases provides mild reaction conditions and low energy cost compared to the chemical process. SGNH-type lipases are very effective catalysts for enzymatic transesterification due to their high reaction rate, great stability, relatively small size for convenient genetic manipulations, and ease of immobilization. Hence, it is highly important to identify novel SGNH-type lipases with high catalytic efficiencies and good stabilities. Results: A promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from Halocynthiibacter arcticus was catalytically characterized and functionally explored. HaSGNH1 displayed broad substrate specificity that included tert-butyl acetate, glucose pentaacetate, and p-nitrophenyl esters with excellent stability and high efficiency. Important amino acids (N83, M86, R87, F131, and I173F) around the substrate-binding pocket were shown to be responsible for catalytic activity, substrate specificity, and reaction kinetics. Moreover, immobilized HaSGNH1 was used to produce high yields of butyl and oleic esters. Conclusions: This work provides a molecular understanding of substrate specificities, catalytic regulation, immobilization, and industrial applications of a promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from H. arcticus. This is the first analysis on biodiesel and flavor synthesis using a cold-adapted halophilic SGNH-type lipase from a Halocynthiibacter species.

show abstract

Section: Characterizations Of Hasgnh1supporting

confidence: 66%

Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus

Yoo

Jeon

et al. 2020

Biotechnol Biofuels

View full text Add to dashboard Cite

show abstract

“…The acetyl xylan esterase AcXE2 (25 kDa) was isolated from Caldicellulosiruptor 494 bescii, a highly thermophilic species able to degrade cellulose (Soni et al, 2017). As an 495 acetyl xylan esterase, AcXE2 removes the acetyl group on acetylated xylobiose and 496 glucose.…”

Section: Family XXXIII 469mentioning

confidence: 99%

Peer Review #2 of "A proposed update for the classification and description of bacterial lipolytic enzymes (v0.1)"

2019

View full text Add to dashboard Cite

Bacterial lipolytic enzymes represent an important class of proteins: they provide their host species with access to additional resources and have multiple applications within the biotechnology sector. Since the formalisation of lipolytic enzymes into families and subfamilies, advances in molecular biology have led to the discovery of lipolytic enzymes unable to be classified via the existing system. Utilising sequence-based comparison methods, we have integrated these novel families within the classification system so that it now consists of 35 families and 11 true lipase subfamilies. Representative sequences for each family and subfamily have been defined as well as methodology for accurate comparison of novel sequences against the reference proteins, facilitating the future assignment of novel proteins. Both the code and protein sequences required for integration of additional families are available at: https://github.com/thh32/Lipase_reclassification. PeerJ reviewing PDF | Abstract 11 12Bacterial lipolytic enzymes represent an important class of proteins: they provide 13 their host species with access to additional resources and have multiple applications 14 within the biotechnology sector. Since the formalisation of lipolytic enzymes into families 15 and subfamilies, advances in molecular biology have led to the discovery of lipolytic 16 enzymes unable to be classified via the existing system. Utilising sequence-based 17 comparison methods, we have integrated these novel families within the classification 18 system so that it now consists of 35 families and 11 true lipase subfamilies. 19 Representative sequences for each family and subfamily have been defined as well as 20 methodology for accurate comparison of novel sequences against the reference 21 proteins, facilitating the future assignment of novel proteins. Both the code and protein 22 sequences required for integration of additional families are available at: 23 https://github.com/thh32/Lipase_reclassification 24 25 26

show abstract

“…The Asp-x-x-His tetrapeptide in motif V constitutes the catalytic machinery of these enzymes. To date, a number of SGNH family esterases have been identified and characterized from several microorganisms [11][12][13][14][15][16][17][18][19], but there are very few reports in lactic acid bacteria.…”

Section: Introductionmentioning

confidence: 99%

Characterization and Immobilization of a Novel SGNH Family Esterase (LaSGNH1) from Lactobacillus acidophilus NCFM

Yoo

Jeon

et al. 2019

IJMS

View full text Add to dashboard Cite

The SGNH family esterases are highly effective biocatalysts due to their strong catalytic efficiencies, great stabilities, relatively small sizes, and ease of immobilization. Here, a novel SGNH family esterase (LaSGNH1) from Lactobacillus acidophilus NCFM, which has homologues in many Lactobacillus species, was identified, characterized, and immobilized. LaSGNH1 is highly active towards acetate-or butyrate-containing compounds, such as p-nitrophenyl acetate or 1-naphthyl acetate. Enzymatic properties of LaSGNH1, including thermal stability, optimum pH, chemical stability, and urea stability, were investigated. Interestingly, LaSGNH1 displayed a wide range of substrate specificity that included glyceryl tributyrate, tert-butyl acetate, and glucose pentaacetate. Furthermore, immobilization of LaSGNH1 by crosslinked enzyme aggregates (CLEAs) showed enhanced thermal stability and efficient recycling property. In summary, this work paves the way for molecular understandings and industrial applications of a novel SGNH family esterase (LaSGNH1) from Lactobacillus acidophilus.

show abstract

SGNH hydrolase-type esterase domain containing Cbes-AcXE2: a novel and thermostable acetyl xylan esterase from Caldicellulosiruptor bescii

Cited by 14 publications

References 50 publications

Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus

Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus

Peer Review #2 of "A proposed update for the classification and description of bacterial lipolytic enzymes (v0.1)"

Characterization and Immobilization of a Novel SGNH Family Esterase (LaSGNH1) from Lactobacillus acidophilus NCFM

Contact Info

Product

Resources

About