Enzymatic modification of wheat starch by a novel maltotetraose-forming amylase from Atopomonas hussainii to retard retrogradation and improve bread quality.

To retard starch retrogradation and improve bread quality, a novel maltotetraose-forming amylase (AhMFA) from Atopomonas hussainii was expressed in Komagataella phaffii. After high cell density fermentation, the enzyme activity reached a maximum level of 3032 U mL. AhMFA showed optimal activity at pH 6.

Simultaneous improvement of thermostability and maltotriose-forming ability of a fungal α-amylase for bread making by directed evolution.

For applications in food industries, a fungal α-amylase from Malbranchea cinnamomea was engineered by directed evolution. Through two rounds of screening, a mutant α-amylase (mMcAmyA) was obtained with higher optimal temperature (70 °C, 5 °C increase) and better hydrolysis properties (18.6 % maltotriose yield, 2.

Synthesis of 2'-fucosyllactose from apple pomace-derived xyloglucan oligosaccharides by an α-L-fucosidase from Pedobacter sp. CAU209.

2'-Fucosyllactose (2'-FL) is known for its ability to provide various health benefits to infants, such as gut maturation, pathogen resistance, improved immunity, and nervous system development. However, the production of 2'-FL using α-L-fucosidases is hindered by the lack of low-cost natural fucosyl donors and high-efficiency α-L-fucosidases. In this work, a recombinant xyloglucanase from Rhizomucor miehei (RmXEG12A) was applied to produce xyloglucan-oligosaccharide (XyG-oligos) from apple pomace.

Tamarind Xyloglucan Oligosaccharides Attenuate Metabolic Disorders via the Gut-Liver Axis in Mice with High-Fat-Diet-Induced Obesity.

Functional oligosaccharides exert obesity-reducing effects by acting at various pathological sites responsible for the development of obesity. In this study, tamarind xyloglucan oligosaccharides (TXOS) were used to attenuate metabolic disorders via the gut-liver axis in mice with high-fat-diet (HFD)-induced obesity, as determined through LC/MS-MS and 16S rRNA sequencing technology. A TXOS dose equivalent to 0.

One-Pot Three-Enzyme System for Production of a Novel Prebiotic Mannosyl-β-(1 → 4)-Fructose Using a d-Mannose Isomerase from .

The present supply of prebiotics is entirely inadequate to meet their demand. To produce novel prebiotics, a d-mannose isomerase (MIaseA) from was first produced in (). MIaseA shared the highest amino acid sequence identity (58.

A novel neutral thermophilic β-mannanase from Malbranchea cinnamomea for controllable production of partially hydrolyzed konjac powder.

Partially hydrolyzed konjac powder (PHKP) can be used to increase the daily intake of dietary fibers of consumers. To produce PHKP by enzymatic hydrolysis, a novel β-mannanase gene (McMan5B) from Malbranchea cinnamomea was expressed in Pichia pastoris. It showed a low identity of less than 52% with other GH family 5 β-mannanases.

Efficient sequential synthesis of lacto-N-triose II and lacto-N-neotetraose by a novel β-N-acetylhexosaminidase from Tyzzerella nexilis.

β-N-acetylhexosaminidases have attracted much attention in recent years due to their potential application in oligosaccharide production, in particular lacto-N-triose II (LNT2) and lacto-N-neotetraose (LNnT) synthesis, which can be further used as backbone precursors for human milk oligosaccharides. A novel β-N-acetylhexosaminidase gene from Tyzzerella nexilis (TnHex189) was heterologously expressed in Bacillus subtilis. The highest β-N-acetylhexosaminidase activity of 14.

Preparation, characterization, and prebiotic activity of manno-oligosaccharides produced from cassia gum by a glycoside hydrolase family 134 β-mannanase.

To produce manno-oligosaccharides from cassia gum, a mutated glycoside hydrolase family 134 β-mannanase gene (mRmMan134A) from Rhizopus microsporus var. rhizopodiformis F518 was expressed in Pichia pastoris and a high expression level (3680 U mL) was obtained through high cell density fermentation. mRmMan134A exhibited maximum activity at pH 5.

A novel high maltose-forming α-amylase from Rhizomucor miehei and its application in the food industry.

A novel α-amylase gene (RmAmyA) from Rhizomucor miehei was cloned and expressed in Pichia pastoris. RmAmyA showed 70% amino acid identity with the α-amylase from Rhizomucor pusillus. A high α-amylase activity of 29,794.

High-level expression of a novel α-amylase from Thermomyces dupontii in Pichia pastoris and its application in maltose syrup production.

A novel α-amylase gene (TdAmyA) with an open reading frame of 1431 bp, deducing 476 amino acids, was cloned from the thermophilic fungus Thermomyces dupontii L18. The recombinant α-amylase was successfully over-expressed in Pichia pastoris. The highest α-amylase activity of 38,314 U/mL was obtained with protein content of 28.

Directed evolution of a β-mannanase from to improve catalytic activity in acidic and thermophilic conditions.

Background: β-Mannanase randomly cleaves the β-1,4-linked mannan backbone of hemicellulose, which plays the most important role in the enzymatic degradation of mannan. Although the industrial applications of β-mannanase have tremendously expanded in recent years, the wild-type β-mannanases are still defective for some industries. The glycoside hydrolase (GH) family 5 β-mannanase (Man5A) from shows many outstanding properties, such as high specific activity and hydrolysis property.

Biochemical properties and application of a novel β-1,3-1,4-glucanase from Paenibacillus barengoltzii.

A novel endo-β-1,3-1,4-glucanase gene (PbBglu16A) was cloned from Paenibacillus barengoltzii and heterogeneously expressed in Escherichia coli. The recombinant β-1,3-1,4-glucanase (PbBglu16A) was purified to homogeneity with a recovery yield of 78.6% and a specific activity of 431.

Comparative analysis on the distribution of protease activities among fruits and vegetable resources.

In this study, a comparative analysis on the distribution of protease activities among 90 plant resources, including fruits and vegetables, has been performed. Protease activities of plant extracts were assayed at different pH values (pH 3.0, pH 7.

Complete genome sequence of the molybdenum-resistant bacterium Bacillus subtilis strain LM 4-2.

Bacillus subtilis LM 4-2, a Gram-positive bacterium was isolated from a molybdenum mine in Luoyang city. Due to its strong resistance to molybdate and potential utilization in bioremediation of molybdate-polluted area, we describe the features of this organism, as well as its complete genome sequence and annotation. The genome was composed of a circular 4,069,266 bp chromosome with average GC content of 43.

Purification and characterization of a chymosin from Rhizopus microsporus var. rhizopodiformis.

Purification and characterization of a chymosin from Rhizopus microsporus var. rhizopodiformis were investigated in the present study. A newly isolated R.

[High-level expression of an extreme-thermostable xylanase B from Thermotoga maritima MSB8 in Escherichia coli and Pichia pastoris].

The family 10 xylanase (XynB) from Thermotoga maritima MSB8 is extremely thermostable and great potential in the applications of various fields of industry. The gene mxynB(64) was amplified by the method of PCR with the template of the genomic DNA of Thermotoga maritima MSB8, and cloned into the expression vectors of Escherichia coli and Pichia pastoris respectively. Xylanase B(40kD) was successfully expressed by the two heterologous protein expression systems with high-level production.

Variation of xylanosomal subunit composition of Streptomyces olivaceoviridis by nitrogen sources.

Besides affecting the xylanases production, different nitrogen sources present in the media also caused changes in the xylanosomal subunit composition of Streptomyces olivaceoviridis E-86. Four xylanosome fractions, purified from the culture supernatant of S. olivaceoviridis E-86 grown on different nitrogen sources, exhibited high specificity towards different xylans and were composed of different subunits.

A novel, ultra-large xylanolytic complex (xylanosome) secreted by Streptomyces olivaceoviridis.

The production of a novel, very large xylanolytic complex (xylanosome) by Streptomyces olivaceoviridis E-86 is reported. The molecular weight was approx. 1200 kDa as determined by native gradient gel electrophoresis.