Purification and Characterization of a Carbohydrate:Acceptor Oxidoreductase fromParaconiothyriumsp. That Produces Lactobionic Acid Efficiently

Kiryu, Takaaki; Nakano, Hirofumi; Kiso, Taro; Murakami, Hiromi

doi:10.1271/bbb.70701

Cited by 36 publications

(25 citation statements)

References 24 publications

(78 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…produced the enzyme in cultivation with a liquid medium containing lactose, peptone, and other nutrients. 14,19) Lactose in the medium promoted the enzyme production. From the culture supernatant, the enzyme was purified by ammonium sulfate precipitation and two steps of anion exchange chromatography.…”

mentioning

confidence: 99%

“…8 10) We also suggested that the sequences of COX and GOOX are highly homologous (40.8%). 9,19) As a result, the former group (CDH and CBQ) is distinguishable from the latter group (COX and GOOX) in the amino acid sequences. Moreover, we found a similarity in the N terminal sequences between the Paraconiothyrium enzyme and COX.…”

mentioning

confidence: 99%

“…Moreover, we found a similarity in the N terminal sequences between the Paraconiothyrium enzyme and COX. 19) Based on the similar sequence as well as the similar specificity for electron donors and acceptors, the Paraconiothyrium enzyme may belong to the enzyme group of COX and GOOX.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Production of Calcium Lactobionate by a Lactose-oxidizing Enzyme from Paraconiothyrium sp. KD-3

et al. 2008

Self Cite

View full text Add to dashboard Cite

A lactose-oxidizing enzyme was obtained from culture supernatant of a fungal strain of Paraconiothyrium sp. KD-3. The enzyme was a flavoprotein with a molecular mass of 54 kDa. The purified enzyme oxidized various monosaccharides and oligosaccharides such as D-glucose, D-galactose, D-xylose, cellooligosaccharides and maltooligosaccharides in addition to lactose, using molecular oxygen as a good electron acceptor, to accumulate the corresponding aldonic acids and hydrogen peroxide. The Paraconiothyrium enzyme was suitable for the production of calcium lactobionate compared with a commercial hexose oxidase owing to the stability during the conversion. The enzyme converted 10 20% (w v) lactose completely to calcium lactobionate in a 500-mL reactor under aeration, agitation and pH regulation at 5.5. The neutralization was successfully performed by the addition of 10% (w w) slurry of calcium carbonate, while neutralization with 25% (w v) sodium hydroxide solution inactivated the enzyme gradually. The supplement of catalase to the mixture promoted the conversion by degrading hydrogen peroxide. The immobilized enzyme, which was prepared by the adsorption to a cation exchange resin followed by the condensation with carbodiimide, oxidized 18.5% (w v) lactose to produce calcium lactobionate in a batch reaction. Calcium lactobionate and aldonates derived from D galactose, D-xylose and L-arabinose showed high aqueous solubility and low calcium binding capability.

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Production of Calcium Lactobionate by a Lactose-oxidizing Enzyme from Paraconiothyrium sp. KD-3

et al. 2008

Self Cite

View full text Add to dashboard Cite

show abstract

“…2) Biological methods using bacteria [3][4][5][6][7][8] and fungi [9][10][11][12][13] have also been studied to produce LacA. However, these microorganisms have also not been applied for the production of LacA for foods, because they are not entirely suitable for industrial production from the perspective of food safety.…”

mentioning

confidence: 99%

Lactobionic and cellobionic acid production profiles of the resting cells of acetic acid bacteria

Kiryu

Kiso

Nakano

et al. 2015

Bioscience, Biotechnology, and Biochemistry

Self Cite

View full text Add to dashboard Cite

Lactobionic acid was produced by acetic acid bacteria to oxidize lactose. Gluconobacter spp. and Gluconacetobacter spp. showed higher lactose-oxidizing activities than Acetobacter spp. Gluconobacter frateurii NBRC3285 produced the highest amount of lactobionic acid per cell, among the strains tested. This bacterium assimilated neither lactose nor lactobionic acid. At high lactose concentration (30%), resting cells of the bacterium showed sufficient oxidizing activity for efficient production of lactobionic acid. These properties may contribute to industrial production of lactobionic acid by the bacterium. The bacterium showed higher oxidizing activity on cellobiose than that on lactose and produced cellobionic acid.

show abstract

“…[1][2][3] It has been reported to increase intestinal calcium absorption, 4,5) suggesting that it might be possible to use LacA for health benefit in foods. There have been a number of studies focusing on lactose-oxidizing bacteria, [6][7][8][9][10][11] fungi, [12][13][14][15][16][17] and red algae. 18) Most of these organisms, however, are difficult to use in the production of LacA for foods.…”

mentioning

confidence: 99%

Optimization of Lactobionic Acid Production byAcetobacter orientalisIsolated from Caucasian Fermented Milk, “Caspian Sea Yogurt”

Kiryu

Yamauchi

Masuyama

et al. 2012

Bioscience, Biotechnology, and Biochemistry

Self Cite

View full text Add to dashboard Cite

Purification and Characterization of a Carbohydrate:Acceptor Oxidoreductase fromParaconiothyriumsp. That Produces Lactobionic Acid Efficiently

Cited by 36 publications

References 24 publications

Production of Calcium Lactobionate by a Lactose-oxidizing Enzyme from <i>Paraconiothyrium</i> sp. KD-3

Production of Calcium Lactobionate by a Lactose-oxidizing Enzyme from <i>Paraconiothyrium</i> sp. KD-3

Lactobionic and cellobionic acid production profiles of the resting cells of acetic acid bacteria

Optimization of Lactobionic Acid Production byAcetobacter orientalisIsolated from Caucasian Fermented Milk, “Caspian Sea Yogurt”

Contact Info

Product

Resources

About