Purification, Characterization and Application of a Cold- Adapted Phospholipase A1 from<i>Bacillus Cereus Sp.</i>AF-1

Zhan, Jianfeng; Jiang, Shaotong; Pan, Lijun; Zhang, Yi

doi:10.5504/bbeq.2013.0044

Cited by 3 publications

(2 citation statements)

References 28 publications

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“…Phospholipids composing plant cell membranes are degraded to lysophospholipids and fatty acids by the lipolytic enzyme phospholipase A, which is secreted by the inoculated microbes [43]. Fatty acids were shown to increase with decomposing triacylglycerol in rice koji fermentation [44].…”

Section: Discussionmentioning

confidence: 99%

Metabolomic Profiles of Aspergillus oryzae and Bacillus amyloliquefaciens During Rice Koji Fermentation

Lee

Jang

et al. 2016

Molecules

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Abstract:Rice koji, used early in the manufacturing process for many fermented foods, produces diverse metabolites and enzymes during fermentation. Using gas chromatography time-of-flight mass spectrometry (GC-TOF-MS), ultrahigh-performance liquid chromatography linear trap quadrupole ion trap tandem mass spectrometry (UHPLC-LTQ-IT-MS/MS), and multivariate analysis we generated the metabolite profiles of rice koji produced by fermentation with Aspergillus oryzae (RK_AO) or Bacillus amyloliquefaciens (RK_BA) for different durations. Two principal components of the metabolomic data distinguished the rice koji samples according to their fermenter species and fermentation time. Several enzymes secreted by the fermenter species, including α-amylase, protease, and β-glucosidase, were assayed to identify differences in expression levels. This approach revealed that carbohydrate metabolism, serine-derived amino acids, and fatty acids were associated with rice koji fermentation by A. oryzae, whereas aromatic and branched chain amino acids, flavonoids, and lysophospholipids were more typical in rice koji fermentation by B. amyloliquefaciens. Antioxidant activity was significantly higher for RK_BA than for RK_AO, as were the abundances of flavonoids, including tricin, tricin glycosides, apigenin glycosides, and chrysoeriol glycosides. In summary, we have used MS-based metabolomics and enzyme activity assays to evaluate the effects of using different microbial species and fermentation times on the nutritional profile of rice koji.

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Section: Discussionmentioning

confidence: 99%

Metabolomic Profiles of Aspergillus oryzae and Bacillus amyloliquefaciens During Rice Koji Fermentation

Lee

Jang

et al. 2016

Molecules

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“…[ 127 ] and from a soil bacterium of Bacillus cereus sp. [ 128 ]. Both of these PLA 1 s have their optimum activity at 35 °C and retain most of their maximal activity at 10 and 4 °C, respectively.…”

Section: Lipase and Phospholipase In Biocatalysismentioning

confidence: 99%

Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications

Borrelli

Trono

2015

IJMS

287

182

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Lipases and phospholipases are interfacial enzymes that hydrolyze hydrophobic ester linkages of triacylglycerols and phospholipids, respectively. In addition to their role as esterases, these enzymes catalyze a plethora of other reactions; indeed, lipases also catalyze esterification, transesterification and interesterification reactions, and phospholipases also show acyltransferase, transacylase and transphosphatidylation activities. Thus, lipases and phospholipases represent versatile biocatalysts that are widely used in various industrial applications, such as for biodiesels, food, nutraceuticals, oil degumming and detergents; minor applications also include bioremediation, agriculture, cosmetics, leather and paper industries. These enzymes are ubiquitous in most living organisms, across animals, plants, yeasts, fungi and bacteria. For their greater availability and their ease of production, microbial lipases and phospholipases are preferred to those derived from animals and plants. Nevertheless, traditional purification strategies from microbe cultures have a number of disadvantages, which include non-reproducibility and low yields. Moreover, native microbial enzymes are not always suitable for biocatalytic processes. The development of molecular techniques for the production of recombinant heterologous proteins in a host system has overcome these constraints, as this allows high-level protein expression and production of new redesigned enzymes with improved catalytic properties. These can meet the requirements of specific industrial process better than the native enzymes. The purpose of this review is to give an overview of the structural and functional features of lipases and phospholipases, to describe the recent advances in optimization of the production of recombinant lipases and phospholipases, and to summarize the information available relating to their major applications in industrial processes.

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Optimization of Phospholipase A1 (PLA1) Production from a Soil Isolate Bacillus subtilis subsp. inaquosorum RG1 via Solid State Fermentation

Kaur¹,

Soni²,

Tewari³

2017

J PURE APPL MICROBIO

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Purification, Characterization and Application of a Cold- Adapted Phospholipase A1 fromBacillus Cereus Sp.AF-1

Cited by 3 publications

References 28 publications

Metabolomic Profiles of Aspergillus oryzae and Bacillus amyloliquefaciens During Rice Koji Fermentation

Metabolomic Profiles of Aspergillus oryzae and Bacillus amyloliquefaciens During Rice Koji Fermentation

Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications

Optimization of Phospholipase A1 (PLA1) Production from a Soil Isolate Bacillus subtilis subsp. inaquosorum RG1 via Solid State Fermentation

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