PMID- 34445200
OWN - NLM
STAT- MEDLINE
DCOM- 20210924
LR  - 20210924
IS  - 1422-0067 (Electronic)
IS  - 1422-0067 (Linking)
VI  - 22
IP  - 16
DP  - 2021 Aug 6
TI  - Biocatalyzed Synthesis of Flavor Esters and Polyesters: A Design of Experiments 
      (DoE) Approach.
LID - 10.3390/ijms22168493 [doi]
LID - 8493
AB  - In the present work, different hydrolases were adsorbed onto polypropylene beads 
      to investigate their activity both in short-esters and polyesters synthesis. The 
      software MODDE((R)) Pro 13 (Sartorius) was used to develop a full-factorial design 
      of experiments (DoE) to analyse the thermostability and selectivity of the 
      immobilized enzyme towards alcohols and acids with different chain lengths in 
      short-esters synthesis reactions. The temperature optima of Candida antarctica 
      lipase B (CaLB), Humicola insolens cutinase (HiC), and Thermobifida 
      cellulosilytica cutinase 1 (Thc_Cut1) were 85  degrees C, 70  degrees C, and 50  degrees C. CaLB and HiC 
      preferred long-chain alcohols and acids as substrate in contrast to Thc_Cut1, 
      which was more active on short-chain monomers. Polymerization of different esters 
      as building blocks was carried out to confirm the applicability of the obtained 
      model on larger macromolecules. The selectivity of both CaLB and HiC was 
      investigated and best results were obtained for dimethyl sebacate (DMSe), leading 
      to polyesters with a M(w) of 18 kDa and 6 kDa. For the polymerization of dimethyl 
      adipate (DMA) with BDO and ODO, higher molecular masses were obtained when using 
      CaLB onto polypropylene beads (CaLB_PP) as compared with CaLB immobilized on 
      macroporous acrylic resin beads (i.e., Novozym 435). Namely, for BDO the M(n) 
      were 7500 and 4300 Da and for ODO 8100 and 5000 Da for CaLB_PP and for the 
      commercial enzymes, respectively. Thc_Cut1 led to polymers with lower molecular 
      masses, with M(n) < 1 kDa. This enzyme showed a temperature optimum of 50  degrees C with 
      63% of DMA and BDO when compared to 54% and 27%, at 70  degrees C and at 85  degrees C, 
      respectively.
FAU - Fabbri, Filippo
AU  - Fabbri F
AUID- ORCID: 0000-0002-8618-6680
AD  - Department of Agrobiotechnology, Institute of Environmental Biotechnology, 
      University of Natural Resources and Life Sciences, Vienna, Konrad Lorenz Strasse 
      20, 3430 Tulln an der Donau, Austria.
FAU - Bertolini, Federico A
AU  - Bertolini FA
AD  - Department of Agrobiotechnology, Institute of Environmental Biotechnology, 
      University of Natural Resources and Life Sciences, Vienna, Konrad Lorenz Strasse 
      20, 3430 Tulln an der Donau, Austria.
FAU - Guebitz, Georg M
AU  - Guebitz GM
AUID- ORCID: 0000-0003-2262-487X
AD  - Department of Agrobiotechnology, Institute of Environmental Biotechnology, 
      University of Natural Resources and Life Sciences, Vienna, Konrad Lorenz Strasse 
      20, 3430 Tulln an der Donau, Austria.
AD  - Austrian Centre of Industrial Biotechnology, Konrad Lorenz Strasse 20, 3430 Tulln 
      an der Donau, Austria.
FAU - Pellis, Alessandro
AU  - Pellis A
AUID- ORCID: 0000-0003-3711-3087
AD  - Department of Agrobiotechnology, Institute of Environmental Biotechnology, 
      University of Natural Resources and Life Sciences, Vienna, Konrad Lorenz Strasse 
      20, 3430 Tulln an der Donau, Austria.
LA  - eng
GR  - n.a./Erasmus+ Traineeship/
PT  - Journal Article
DEP - 20210806
PL  - Switzerland
TA  - Int J Mol Sci
JT  - International journal of molecular sciences
JID - 101092791
RN  - 0 (Enzymes, Immobilized)
RN  - 0 (Esters)
RN  - 0 (Flavoring Agents)
RN  - 0 (Fungal Proteins)
RN  - 0 (Polyesters)
RN  - EC 3.1.1.- (Carboxylic Ester Hydrolases)
RN  - EC 3.1.1.- (cutinase)
RN  - EC 3.1.1.3 (Lipase)
RN  - EC 3.1.1.3 (lipase B, Candida antarctica)
RN  - Thermobifida cellulosilytica
SB  - IM
MH  - Biocatalysis
MH  - Candida/enzymology
MH  - Carboxylic Ester Hydrolases/chemistry
MH  - Enzymes, Immobilized/chemistry
MH  - Esters/*chemical synthesis
MH  - Flavoring Agents/*chemical synthesis
MH  - Fungal Genus Humicola/enzymology
MH  - Fungal Proteins/chemistry
MH  - Lipase/chemistry
MH  - Polyesters/*chemical synthesis
MH  - Polymerization
MH  - Thermobifida/enzymology
PMC - PMC8395215
OTO - NOTNLM
OT  - bioplastics
OT  - closure of the carbon cycle
OT  - design of experiments
OT  - flavor esters synthesis
OT  - hydrolytic enzymes
OT  - polyesters synthesis
COIS- The authors declare no conflict of interest.
EDAT- 2021/08/28 06:00
MHDA- 2021/09/25 06:00
PMCR- 2021/08/06
CRDT- 2021/08/27 01:23
PHST- 2021/07/05 00:00 [received]
PHST- 2021/08/04 00:00 [revised]
PHST- 2021/08/04 00:00 [accepted]
PHST- 2021/08/27 01:23 [entrez]
PHST- 2021/08/28 06:00 [pubmed]
PHST- 2021/09/25 06:00 [medline]
PHST- 2021/08/06 00:00 [pmc-release]
AID - ijms22168493 [pii]
AID - ijms-22-08493 [pii]
AID - 10.3390/ijms22168493 [doi]
PST - epublish
SO  - Int J Mol Sci. 2021 Aug 6;22(16):8493. doi: 10.3390/ijms22168493.