scholarly journals Preparation and immobilization Glucoamylase and Pectinase by CLEA method

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.

scholarly journals Safety Evaluation and Whole Genome Sequencing of Aspergillus japonicas PJ01 Reveal Its Potential to Degrade Citrus Segments in Juice Processing

Foods ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1736
Author(s):  
Yujiao Qian ◽  
Zhipeng Gao ◽  
Jieyi Wang ◽  
Chen Wang ◽  
Gaoyang Li ◽  
...  
Keyword(s):  
Whole Genome Sequencing ◽  
Genome Sequencing ◽  
Gene Annotation ◽  
Gc Content ◽  
Crude Enzyme ◽  
Control Group ◽  
Whole Genome ◽  
Enzyme Solution ◽  
Juice Processing ◽  
Crude Enzyme Solution

Aspergillus japonicas PJ01 (A. japonicas PJ01) is a strain isolated from the rotten branches. In previ-ous studies, it was shown that it can produce complex enzymes to degrade polysaccharide com-ponents. In this study, we evaluated the safety of its crude enzyme solution. Acute oral toxicity, subchronic toxicity, micronucleus and sperm malformation tests all validated the high biologi-cal safety for the crude enzymes. Secondly, we carried out the citrus segment degradation ex-periment of crude enzyme solution. Compared with the control group, the crude enzyme solu-tion of A. japonicas PJ01 can completely degrade the segments in 50 min, which provides the basis for enzymatic peeling during juice processing. The whole genome sequencing showed that the genome of A. japonicus PJ01 has a GC content of 51.37% with a size of 36204647 bp, and encoded 10070 genes. GO, COG, KEGG and CAZy databases were used in gene annotation analyses. Pathway enrichment showed many genes related to carbohydrate metabolism, rich in genes re-lated to pectinase, xylanase and carboxylcellulase. Therefore, the complex enzyme produced by A. japonicus PJ01 can be used in gizzard juice processing to achieve efficient enzymatic decapsu-lation.

scholarly journals Enzyme-Assisted Method for Phycobiliproteins Extraction from Porphyra and Evaluation of Their Bioactivity

Processes ◽  
2021 ◽  
Vol 9 (3) ◽  
pp. 560
Author(s):  
Chung-Hsiung Huang ◽  
Wei-Chen Chen ◽  
Yu-Huei Gao ◽  
Guan-Wen Chen ◽  
Hong-Ting Victor Lin ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Enzymatic Hydrolysis ◽  
Antioxidant Activities ◽  
Polyacrylamide Gel Electrophoresis ◽  
Radical Scavenging ◽  
Crude Enzyme ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Enzyme Solution ◽  
Crude Enzyme Solution

Due to the poor protein availability of algae in their unprocessed form, development of extraction methods for phycobiliproteins is of great significance. This study aimed to extract phycoerythrin (PE) and phycocyanin (PC) from Porphyra via bacterial enzymatic hydrolysis and to evaluate their bioactivity. To induce enzyme production, Porphyra powder was added into the culture medium of two marine bacterial strains. The pH and enzyme activity of the cultured supernatant, namely crude enzyme solution, were significantly raised. For PE and PC extraction, Porphyra were incubated within crude enzyme solution with homogenization and ultrasonication followed by ultrafiltration process. After distinguishing by fast performance liquid chromatography (FPLC), three major fractions were observed and identified as R-PE, R-PC and small molecular PE by high-performance liquid chromatography (HPLC) and polyacrylamide gel electrophoresis (PAGE) analysis. With respect to bioactivity, these three fractions exhibited free radical scavenging and antioxidant activities in a various degree. In addition, the angiotensin-converting-enzyme (ACE) inhibitory activity of both R-PE and R-PC fractions was observed in a concentration-dependent manner. Taken together, the employed process of bacterial enzymatic hydrolysis is suggested to be a feasible method to obtain PE and PC from Porphyra without limiting their bioactivity.

Production and Properties of a Bacterial Thermostable Exo-inulinase

2001 ◽  
Vol 56 (11-12) ◽  
pp. 1022-1028 ◽  
Author(s):  
Kristina Uzunova ◽  
Anna Vassileva ◽  
Margarita Kambourova ◽  
Viara Ivanova ◽  
Dimitrina Spasova ◽  
...  
Keyword(s):  
Enzyme Production ◽  
Enzyme Preparation ◽  
Batch Cultivation ◽  
Crude Enzyme ◽  
Growth Time ◽  
Bacillus Sp ◽  
High Thermostability ◽  
Crude Enzyme Preparation ◽  
Ph Range

Abstract Enzyme production of newly isolated thermophilic inulin-degrading Bacillus sp. 11 strain was studied by batch cultivation in a fermentor. The achieved inulinase and invertase activi­ ties after a short growth time (4.25 h) were similar or higher compared to those reported for other mesophilic aerobic or anaerobic thermophilic bacterial producers and yeasts. The investigated enzyme belonged to the exo-type inulinases and splitted-off inulin, sucrose and raffinose. It could be used at temperatures above 65 °C and pH range 5.5-7.5. The obtained crude enzyme preparation possessed high thermostability. The residual inulinase and inver­ tase activities were 92-98% after pretreatment at 65 °C for 60 min in the presence of substrate inulin.

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