A novel family of glucosyl 1,5-anhydro-d-fructose derivatives synthesised by transglucosylation with dextransucrase from Leuconostoc mesenteroides NRRL B-512F

1,5-Anhydro-d-fructose (AF), a metabolite of starch/glycogen degradation, is a good antioxidant. With the prospect of increasing its applications and use as a food ingredient, AF glucosylation catalysed by the dextransucrase from Leuconostoc mesenteroides NRRL B-512F was performed in the presence of sucrose. This led to AF glucosylated derivatives containing alpha-(1-->6) linkages named 1,5-anhydro-d-fructo-glucooligosaccharides (AFGOS). LC-MS analyses showed that AFGOS with a degree of polymerisation (DP) of up to 7 were synthesised. The amount of AFGOS produced and the average DP increased by using a high sucrose/AF molar ratio and high total sugar concentration. AFGOS were proved to present antioxidant properties quite similar to AF.     

Cloning and characterization of the bifunctional alcohol/acetaldehyde dehydrogenase gene (<Emphasis Type="BoldItalic">adhE</Emphasis>) in <Emphasis Type="BoldItalic">Leuconostoc mesenteroides</Emphasis> isolated from kimchi

A bifunctional alcohol/acetaldehyde dehydrogenase (AdhE) gene (adhE) was cloned from Leuconostoc mesenteroides C7 (LMC7), which is the dominant lactic acid bacterium produced during heterofermentation of kimchi. The nucleotide sequence of the DNA fragment containing putative adhE, which is 2685 bp long and encodes an 886 amino acid polypeptide, exhibits 99% homology with Leu. mesenteroides sp. cremoris. The deduced AdhE comprises two conserved domains: alcohol dehydrogenase (Adh) and acetaldehyde dehydrogenase (Aldh). Moreover, two NAD-binding sites were observed, based on the presence of the GXGXXG motif. A pADHE containing the adhE gene expressed AdhE at the translational level in Escherichia coli BL21, which was at a higher level than in E. coli DH5 and E. coli JM109. The AdhE of LMC7 showed Adh and Aldh activities that, when expressed in E. coli. BL21, were 7.5 and 5.7 U mg^-1 , respectively.     

葡萄酒苹果酸—乳酸发酵接种时间选择的研究

分别在佳利酿葡萄汁酒精发酵前期（第Ｉ阶段）、中后期（第Ⅱ阶段）和结束时（第Ⅲ阶段）接种酒明串珠菌（Ｌｅｕｃｏｎｏｓｔｏｃ ｏｅｎｏｓ）３１ＤＨ,进行苹果酸－乳酸发酵（ＭＬＦ）接种时间选择的研究,结果表明：不同阶段接种经ＭＬＦ后总酸降幅均为２．６ｇ／Ｌ;挥发酸含量上升且第Ｉ阶段＞第Ⅱ阶段＞第Ⅲ阶段;挥发酯以第Ⅱ阶段含量最高,为０．３７ｇ／Ｌ,同其他两阶段含量相比较,差异显（α＝０．０５）;接种时间     

Search for a dextransucrase minimal motif involved in dextran binding

Fourteen truncated forms of Leuconostoc mesenteroides NRRL B512-F dextransucrase, involving N-, C- or N- plus C-terminal domain truncations were tested for their ability to bind dextrans. The shortest fragment (14kDa molecular weight) that still exhibited a strong interaction with dextran was localized between amino acids N1397 and A1527 of the C-terminal domain (GBD-7) and consists of six YG repeats. With a dissociation constant K(d) of 2.8x10(-9)M, this motif shows a very high affinity for isomaltohexaose and longer dextrans, supporting the proposed role of GBD in polymer formation. The potential application of GBD-7 as an affinity tag onto cheap resins like Sephacryl S300HR for rapid purification was evaluated and is discussed.     

An overview of purification methods of glycoside hydrolase family 70 dextransucrase

The enzyme dextransucrase (sucrose:1, 6-α-D-glucan 6-α-glucosyltransferase, EC 2.4.1.5) catalyses the synthesis of exopolysaccharide, dextran from sucrose. This class of polysaccharide has been extensively exploited in pharmaceutical industry as blood volume expander, as stabiliser in food industry and as a chromatographic medium in fine chemical industry because of their nonionic nature and stability. Majority of the dextrans are synthesized from sucrose by dextransucrase secreted mainly by bacteria belonging to genera Leuconostoc, Streptococcus and Lactobacillus. Bulk of the information on purification of extracellular dextransucrase has been generated from Leuconostoc species. Various methods such as precipitation by ammonium sulphate, ethanol or polyethylene glycol, phase partitioning, ultrafiltration and chromatography have been used to purify the enzyme. Purification of dextransucrase is rendered difficult by the presence of viscous dextran in the medium. However, processes like ultra-filtration, salt and PEG precipitation, chromatography and phase partitioning have been standardized and successfully used for higher scale purification of the enzyme. A recombinant dextransucrase from Leuconostoc mesenteroides B-512F with a histidine tag has been expressed in E. coli cells and purifi ed by immobilized metal ion chromatography. This review reports the available information on purifi cation methods of dextransucrase from Leuconostoc mesenteroides strains.     

肠膜明串珠菌右旋糖苷蔗糖酶的研究进展

综述了肠膜明串珠菌(Leuconostoc mesnteroides)右旋糖苷蔗糖酶结构、作用机制、基因克隆与表达研究进展。     

L.SP.HXQ001菌对家兔血清胆固醇的影响

目的 探讨乳酸细菌中的明串珠菌对血清胆固醇的影响。方法 通过给实验性高胆固醇血症家兔喂L.sp.HXQ001菌液,测定其血清胆固醇含量,并与持续高脂喂饲、停高脂喂饲后自然降低血清胆固醇比较,分析其对脂代谢的影响。结果 L.sp.HXQ001菌有预防高脂饲料所引发的高胆固醇血症作用,对实验性高胆固醇血症有较好的降低血清胆醇作用。结论：L.sp.HXQ001菌显示有较好的调节血清胆固醇作用,有可能成为新的微生态调节剂,并在防治高胆固醇血症方面发挥作用。