D-Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum L-arabinose isomerase

N. Salonen (Corresponding Author), K. Salonen, M. Leisola, Antti Nyyssölä

Research output: Contribution to journalArticleScientificpeer-review

18 Citations (Scopus)

Abstract

Bifidobacterium longum NRRL B-41409 l-arabinose isomerase (l-AI) was overexpressed in Lactococcus lactis using a phosphate depletion inducible expression system. The resting L. lactis cells harboring the B. longum l-AI were used for production of d-tagatose from d-galactose in the presence of borate buffer. Multivariable analysis suggested that high pH, temperature and borate concentration favoured the conversion of d-galactose to d-tagatose. Almost quantitative conversion (92 %) was achieved at 20 g L−1 substrate and at 37.5 °C after 5 days. The d-tagatose production rate of 185 g L−1 day−1 was obtained at 300 g L−1 galactose, at 1.15 M borate, and at 41 °C during 10 days when the production medium was changed every 24 h. There was no significant loss in productivity during ten sequential 24 h batches. The initial d-tagatose production rate was 290 g L−1 day−1 under these conditions.
Original languageEnglish
Pages (from-to)489-497
Number of pages9
JournalBioprocess and Biosystems Engineering
Volume36
Issue number4
DOIs
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed

Fingerprint

L-arabinose isomerase
Lactococcus lactis
Borates
Galactose
Isomerases
Arabinose
Buffers
Phosphates
Productivity
Temperature
tagatose
Bifidobacterium longum
Substrates

Keywords

  • Bifidobacterium longum
  • borate
  • d-tagatose
  • l-arabinose isomerase
  • Lactococcus lactis
  • resting cells

Cite this

@article{814ad108ae7b4c73b10c50606f565519,
title = "D-Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum L-arabinose isomerase",
abstract = "Bifidobacterium longum NRRL B-41409 l-arabinose isomerase (l-AI) was overexpressed in Lactococcus lactis using a phosphate depletion inducible expression system. The resting L. lactis cells harboring the B. longum l-AI were used for production of d-tagatose from d-galactose in the presence of borate buffer. Multivariable analysis suggested that high pH, temperature and borate concentration favoured the conversion of d-galactose to d-tagatose. Almost quantitative conversion (92 {\%}) was achieved at 20 g L−1 substrate and at 37.5 °C after 5 days. The d-tagatose production rate of 185 g L−1 day−1 was obtained at 300 g L−1 galactose, at 1.15 M borate, and at 41 °C during 10 days when the production medium was changed every 24 h. There was no significant loss in productivity during ten sequential 24 h batches. The initial d-tagatose production rate was 290 g L−1 day−1 under these conditions.",
keywords = "Bifidobacterium longum, borate, d-tagatose, l-arabinose isomerase, Lactococcus lactis, resting cells",
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D-Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum L-arabinose isomerase. / Salonen, N. (Corresponding Author); Salonen, K.; Leisola, M.; Nyyssölä, Antti.

In: Bioprocess and Biosystems Engineering, Vol. 36, No. 4, 2013, p. 489-497.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - D-Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum L-arabinose isomerase

AU - Salonen, N.

AU - Salonen, K.

AU - Leisola, M.

AU - Nyyssölä, Antti

PY - 2013

Y1 - 2013

N2 - Bifidobacterium longum NRRL B-41409 l-arabinose isomerase (l-AI) was overexpressed in Lactococcus lactis using a phosphate depletion inducible expression system. The resting L. lactis cells harboring the B. longum l-AI were used for production of d-tagatose from d-galactose in the presence of borate buffer. Multivariable analysis suggested that high pH, temperature and borate concentration favoured the conversion of d-galactose to d-tagatose. Almost quantitative conversion (92 %) was achieved at 20 g L−1 substrate and at 37.5 °C after 5 days. The d-tagatose production rate of 185 g L−1 day−1 was obtained at 300 g L−1 galactose, at 1.15 M borate, and at 41 °C during 10 days when the production medium was changed every 24 h. There was no significant loss in productivity during ten sequential 24 h batches. The initial d-tagatose production rate was 290 g L−1 day−1 under these conditions.

AB - Bifidobacterium longum NRRL B-41409 l-arabinose isomerase (l-AI) was overexpressed in Lactococcus lactis using a phosphate depletion inducible expression system. The resting L. lactis cells harboring the B. longum l-AI were used for production of d-tagatose from d-galactose in the presence of borate buffer. Multivariable analysis suggested that high pH, temperature and borate concentration favoured the conversion of d-galactose to d-tagatose. Almost quantitative conversion (92 %) was achieved at 20 g L−1 substrate and at 37.5 °C after 5 days. The d-tagatose production rate of 185 g L−1 day−1 was obtained at 300 g L−1 galactose, at 1.15 M borate, and at 41 °C during 10 days when the production medium was changed every 24 h. There was no significant loss in productivity during ten sequential 24 h batches. The initial d-tagatose production rate was 290 g L−1 day−1 under these conditions.

KW - Bifidobacterium longum

KW - borate

KW - d-tagatose

KW - l-arabinose isomerase

KW - Lactococcus lactis

KW - resting cells

U2 - 10.1007/s00449-012-0805-2

DO - 10.1007/s00449-012-0805-2

M3 - Article

VL - 36

SP - 489

EP - 497

JO - Bioprocess and Biosystems Engineering

JF - Bioprocess and Biosystems Engineering

SN - 1615-7591

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