Safety Evaluation of Amino Peptidase Enzyme Preparation derived from Aspergillus niger

Growth of Aspergillus niger in the presence of [2-14C]mevalonate and 32Pi led to the formation of a lipid, containing 14C (0.14% of dose) and 32P (0.009% of dose), that had chromatographic properties identical with those of exo-methylene-hexahydropolyprenol phosphate. When a particulate enzyme preparation from the thallus of A. niger was incubated with GDP-[14C]mannose, the main radioactive products were mannose 1-phosphate (57% of products) and mannose (18%). In addition radioactive mannan (8%) and a mannolipid (2%) were formed. The latter was identified as exo-methylene-hexahydropolyprenol phosphate mannose on the basis of its chromatographic properties, acid lability and on the increase in formation of the mannolipid when the phosphate of exo-methylene-hexahydropolyprenols was added to the incubation mixture. The phosphates of ficaprenols and cetyl alcohol caused no corresponding increase. These observations are interpreted as evidence that the thallus of A. niger contains a mannose transferase that uses the phosphate of exo-methylene-hexahydropolyprenols as an acceptor. This situation is discussed in the light of the analogous involvement of a prenol phosphate mannose as an intermediate in the biosynthesis of bacterial wall mannan.

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A novel multi-enzyme preparation produced from Aspergillus niger using biodegradable waste: a possible option to combat heterogeneous biofilms

AMB Express ◽

10.1186/s13568-020-00970-3 ◽

2020 ◽

Vol 10 (1) ◽

Cited By ~ 1

Author(s):

Arashdeep Kaur ◽

Valbha Rishi ◽

Sanjeev Kumar Soni ◽

Praveen Rishi

Keyword(s):

Aspergillus Niger ◽

Enzyme Preparation ◽

Biodegradable Waste

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Purification and Characterization of Two β-d-Glucosidases from an Aspergillus Niger Enzyme Preparation: Affinity and Specificity Toward Glucosylated Compounds Characteristic of the Processing of Fruits

Enzyme and Microbial Technology ◽

10.1016/s0141-0229(97)00206-8 ◽

1998 ◽

Vol 22 (5) ◽

pp. 374-382 ◽

Cited By ~ 29

Author(s):

Marie-Paule Le Traon-Masson ◽

Patrice Pellerin

Keyword(s):

Aspergillus Niger ◽

Enzyme Preparation ◽

Purification And Characterization

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Multiple forms of glycosidases in an enzyme preparation from Aspergillus niger: Partial characterization of a β-apiosidase

Enzyme and Microbial Technology ◽

10.1016/s0141-0229(96)00221-9 ◽

1997 ◽

Vol 21 (1) ◽

pp. 39-44 ◽

Cited By ~ 16

Author(s):

Ziya Günata ◽

Isabelle Dugelay ◽

M.J. Vallier ◽

J.C. Sapis ◽

C. Bayonove

Keyword(s):

Aspergillus Niger ◽

Enzyme Preparation ◽

Partial Characterization ◽

Multiple Forms

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Safety evaluation of a food enzyme with glucan 1,4‐α‐glucosidase and α‐amylase activities from the genetically modified Aspergillus niger strain NZYM‐BX

EFSA Journal ◽

10.2903/j.efsa.2021.6563 ◽

2021 ◽

Vol 19 (5) ◽

Author(s):

◽

Claude Lambré ◽

José Manuel Barat Baviera ◽

Claudia Bolognesi ◽

Pier Sandro Cocconcelli ◽

...

Keyword(s):

Aspergillus Niger ◽

Genetically Modified ◽

Safety Evaluation

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Preparation and immobilization Glucoamylase and Pectinase by CLEA method

Science and Technology Development Journal ◽

10.32508/stdj.v17i2.1358 ◽

2014 ◽

Vol 17 (2) ◽

pp. 45-51

Author(s):

Giang Thi Linh Tran ◽

Oanh Ngoc Huynh

Keyword(s):

Aspergillus Niger ◽

Enzyme Preparation ◽

Immobilized Enzyme ◽

Solution Culture ◽

Crude Enzyme ◽

Cross Linking ◽

Solid Culture ◽

Enzyme Solution ◽

Crude Enzyme Solution ◽

Semi Solid

CLEA method (cross-linking enzyme aggregates) combines enzyme preparation and immobilization from solution culture into the same step. In this study, we applied CLEA method to immobilize two enzymes, glucoamylase and pectinase, from crude enzyme solution obtained from semi-solid culture of Aspergillus niger. The results showed that: In the same immobilized conditions (glucoamylase: 7% glutaraldehyde, 5°C, 2 hours; pectinase: 10% glutaraldehyde, 5°C, 2 hours), the immobilized enzyme from crude enzyme solution, has the abilities to be reused and activation stability under the influences of pH and temperature higher than immobilized commercial enzyme respectively.

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