Pectinase Production by Aspergillus niger and Its Applications in Fruit Juice Clarification

نویسندگان

چکیده

Pectinases (EC 3.2.1.15) are a class of enzymes that catalyze the depolymerization or de-esterification reactions degrade pectic substances. In present study, we have isolated Aspergillus niger strain from soil samples, in India and evaluated pectinase production. The highest producing A. was further optimized with various agricultural wastes. Plackett-Burman design (PBD) Central composite ‘(CCD)’ were used to determine best parameters for maximum Pectinase activity increased 99.21 U/ml after optimizing production medium using PBD CCD statistical analysis. A positive correlation between predicted (112.65 U/ml) experimental (99.21 SD=0.005) optimum observed. Maximum produced by under submerged fermentation, utilizing orange peel, which is cost-effective, adaptable, environmentally friendly approach. partially purified showed significant application apple juice clarification ability pectin therefore colour change observed within 120 min. waste peel fermentation an economical, versatile eco-friendly process clarification.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

An acidic pectin lyase from Aspergillus niger with favourable efficiency in fruit juice clarification.

The pectin lyase gene pnl-zj5a from Aspergillus niger ZJ5 was identified and expressed in Pichia pastoris. PNL-ZJ5A was purified by ultrafiltration, anion exchange and gel chromatography. The Km and Vmax values determined using citrus pectin were 0.66 mg ml(-1) and 32.6 μmol min(-1) mg(-1) , respectively. PNL-ZJ5A exhibited optimal activity at 43°C and retained activity over 25-50°C. PNL-ZJ5A w...

متن کامل

Production kinetics and characterization of pectinase enzyme from Aspergillus niger

Food grade pectinases from Aspergillus niger are predominantly used as processing aids in industries. In the present investigation, efforts towards standardization for pilot scale production of pectinase enzyme from A. niger were made. The crude enzyme was studied for its kinetics to optimize substrate concentration and processing parameters on the basis of polygalacturonic activity. Km (Michae...

متن کامل

Purification and characterization of pectinase produced from Apple pomace and evaluation of its efficacy in fruit juice extraction and clarification

Pectinase (Pectin methyl esterase) produced by Aspergillus niger in solid state fermentation of apple pomace using the optimized conditions was partially purified by (NH4)2SO4 fractionation (20-80% concentration). The purified enzyme was found to be stable up to 60 days. It remained heat stable up to 50oC but completely inactivated at 90oC. The partially purified enzyme showed highest activity ...

متن کامل

Exploitation of Fruit Wastes for Pectinase Production Using Aspergillus Oryzae

Ever increasing population and industrialization has resulted in heavy pollution and waste generation. The main aim of this project lies in waste management and synthesis of pectinase enzyme which plays a crucial role in sewage treatment. Twenty moulds were isolated from decaying fruits and municipal waste soil sample on SDA and were further screened for pectinolytic enzyme production. Screenin...

متن کامل

Affinity precipitation of Aspergillus niger pectinase by microwave-treated alginate.

Affinity precipitation is a simple, single plate separation process in which the complex of a smart macroaffinity ligand with the target protein (from a crude broth) can be selectively precipitated by application of a suitable stimulus. Alginate is a copolymer of guluronic acid and mannuronic acid residues and precipitates with Ca(2+) ions. It was found to bind to pectinase present in a commerc...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Journal of Pure and Applied Microbiology

سال: 2022

ISSN: ['2581-690X', '0973-7510']

DOI: https://doi.org/10.22207/jpam.16.4.43