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Journal ArticleDOI

Studies on pH and thermal deactivation of pectolytic enzymes from Aspergillus niger

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TLDR
The addition of protein doubled the half-life times of partially purified PMG, PG I and PG II and the interaction effect of pectolytic enzymes on deactivation was found to be significant.
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This article is published in Biochemical Engineering Journal.The article was published on 2003-10-01. It has received 108 citations till now.

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Journal ArticleDOI

Pectin and Pectinases: Production, Characterization and Industrial Application of Microbial Pectinolytic Enzymes

TL;DR: Departamento de Bioquimica e Microbiologia Instituto de Biociencias Universidade Estadual Paulista, UNESP, Avenida 24A, 1515, CEP 13506-900 Rio Claro, SP
Journal ArticleDOI

Microbial pectinase: sources, characterization and applications

TL;DR: This paper provides a bird’s eye view of the possible application of these enzymes in commercial sector and the molecular characterization of pectinolytic enzymes.
Journal ArticleDOI

Purification and characterization of glutaminase-free l-asparaginase from Pectobacterium carotovorum MTCC 1428

TL;DR: The purified L-asparaginase has no partial glutaminase activity, which can reduce the possibility of side effects during the course of anti-cancer therapy, and is moderately inhibited by various divalent cations and thiol group blocking reagents.
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Kinetic properties and thermal behaviour of polygalacturonase used in fruit juice clarification

TL;DR: In this article, thermal inactivation curves were not linear in the range 40-60 °C and the optimum pH for enzyme activity was 4.7 for Pectinex 3XL and 4.0 for both Rapidase C80 and Pectinase CCM.
Journal ArticleDOI

Use of pectinases produced by a new strain of Aspergillus niger for the enzymatic treatment of apple and blueberry juice

TL;DR: In this article, pectinases-producing filamentous fungi were isolated with the aim of using their enzymes in the clarification of apple and blueberry juices, and the experimental extract enzyme EE obtained in solid-state process with a strain identified as belonging to the species Aspergillus niger and designated LB23 was used for treating juices and compared with two commercial enzyme preparations.
References
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Journal ArticleDOI

Statistical optimization of medium components for improved synthesis of pectinase by Aspergillus niger

TL;DR: In this article, the synthesis of pectinase using Aspergillus niger, NCIM 548, has been enhanced by optimizing the carbon and nitrogen sources present in the medium.
Journal ArticleDOI

Performance of pectolytic enzymes during hydrolysis of pectic substances under assay conditions: a statistical approach

TL;DR: In this paper, reaction conditions were optimized for enzymatic hydrolysis of pectic substances using pectolytic enzymes produced by Aspergillus niger NCIM 548.
Journal ArticleDOI

Application of response surface methodology to evaluate some aspects on stability of pectolytic enzymes from Aspergillus niger

TL;DR: In this article, the combined effect of pH and temperature on these enzymes was studied using response surface methodology, and it was found that pectinlyase is more thermostable than other two enzymes.
Journal ArticleDOI

Production of pectolytic enzymes by Aspergillus niger: effect of inoculum size and potassium hexacyanoferrate II-trihydrate

TL;DR: A pronounced effect of KHCF on fungal morphology as well as on enzymatic activity was observed, and with increased concentration the morphology gradually changed from loose pellets to smaller compact ones.
Journal ArticleDOI

The pectic enzymes of Aspergillus niger. A second exopolygalacturonase

PJ Mill
- 01 Jun 1966 - 
TL;DR: A second exopolygalacturonase was separated from a mycelial extract of Aspergillus niger with a 265-fold purification and a recovery of 1% and showed no requirement for metal activators, nor was it inhibited by chelating agents.
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