Immobilization studies of a pectinase produced by Aspergillus terreus

Abstract

Aspergillus terreus can produce different holocellulose‐degrading enzymes when grown in sugarcane bagasse, with predominant pectinase activity. Thus, pectinase was selected for purification and immobilization studies. Ion exchange and molecular exclusion chromatography studies were performed, after which it was possible to semipurify the enzyme with a yield of 80%. The crude extract pectinase (PECEB) and the partially purified enzyme (PEC2) were immobilized on monoamino‐N‐aminoethyl (MANAE)‐agarose with pectinase activity yields of 66% and 98%, respectively. After immobilization in MANAE‐agarose, the pectinase showed higher activity at acidic pH (pH 4.0) when compared to the nonimmobilized enzyme. It was also found that after the immobilization process, there was a threefold improvement in the enzyme's thermostability. Also, it was possible to reuse the immobilized enzyme for up to five cycles of hydrolysis with effective production of reducing sugars (0.196 mg/g of substrate). The industrial application test revealed a significant decrease in the viscosity of guava juice when the immobilized enzyme was used. PECEB, immobilized on MANAE‐agarose, was the enzyme sample that generated the highest pulp viscosity reduction (approximately 47%). Although additional studies are needed for practical industrial application, the results obtained herein reveal the potential of application of immobilized pectinase in the industry.

Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential

“…22 Similarly, a semi-purification process applied to polygalacturonase from A. japonicas 23 resulted in a 2.8-fold purification after two chromatography steps, which is similar to the semi-purified polygalacturonase from A. terreus with yields of 2.5% and 6.2%, respectively. 24 These comparative results emphasise the effectiveness of the applied purification strategy in achieving a considerable purification fold for the polygalacturonase of interest, with a competitive yield and specific activity.…”

“…A study by da Câmara Rocha et al (2020) showed that A. niger exhibits sustained PG activity over 2 h at 30 °C and 40 °C within the pH range of 4.0-6.0. 32 Similarly, Vaz et al (2021) reported that the PG of A. terreus reaches its half-life after 2 h of incubation at 40 °C, 24 mirroring the behaviour observed in the PG from A. japonicus at 50 °C. 23 However, the mandatory transition to PG variants for industrial applications requires an improvement in thermostability.…”

A cleaning and reusable biochemical degumming method for hemp fibers through immobilized pectinase lyase on calcium alginate microspheres

“…14 To overcome the above problems and the difficulties of separation, purification, recycling and utilization, immobilized enzymes have become the current basis of research into enzyme degumming. 15,16 The immobilized enzyme can still exhibit its unique catalytic function when a carrier material is used to confine or immobilize the enzyme in a specific area. Compared with the free enzyme, the immobilized enzyme can be reused many times and is easy to separate and recycle.…”