A comprehensive review on incredible renewable carriers as promising platforms for enzyme immobilization & thereof strategies
Enzymes are the highly versatile bio-catalysts having the potential for being employed in
biotechnological and industrial sectors to catalyze biosynthetic reactions over a commercial …
biotechnological and industrial sectors to catalyze biosynthetic reactions over a commercial …
From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymes
Enzymes found in nature have been exploited in industry due to their inherent catalytic
properties in complex chemical processes under mild experimental and environmental …
properties in complex chemical processes under mild experimental and environmental …
Application of immobilized enzymes in food industry
ED Yushkova, EA Nazarova… - Journal of agricultural …, 2019 - ACS Publications
Enzymes are macromolecular biocatalysts, widely used in food industry. In applications,
enzymes are often immobilized on inert and insoluble carriers, which increase their …
enzymes are often immobilized on inert and insoluble carriers, which increase their …
Enzyme immobilization onto renewable polymeric matrixes: Past, present, and future trends
CS Bezerra, CMG de Farias Lemos… - Journal of Applied …, 2015 - Wiley Online Library
In this review, we present an overview of the different renewable polymers that are currently
being used as matrixes for enzyme immobilization and their properties and of new …
being used as matrixes for enzyme immobilization and their properties and of new …
Solvent tolerant enzymes in extremophiles: adaptations and applications
Non-aqueous enzymology has always drawn attention due to the wide range of unique
possibilities in biocatalysis. In general, the enzymes do not or insignificantly catalyze …
possibilities in biocatalysis. In general, the enzymes do not or insignificantly catalyze …
Amylases from thermophilic bacteria: structure and function relationship
Amylases hydrolyze starch to diverse products including dextrins and progressively smaller
polymers of glucose units. Thermally stable amylases account for nearly 25% of the enzyme …
polymers of glucose units. Thermally stable amylases account for nearly 25% of the enzyme …
Bioremediation of pesticide contaminated water using an organophosphate degrading enzyme immobilized on nonwoven polyester textiles
Bioremediation using enzymes has become an attractive approach for removing hazardous
chemicals such as organophosphate pesticides from the environment. Enzymes …
chemicals such as organophosphate pesticides from the environment. Enzymes …
Covalent immobilization of peanut β-amylase for producing industrial nano-biocatalysts: a comparative study of kinetics, stability and reusability of the immobilized …
R Das, M Talat, ON Srivastava, AM Kayastha - Food chemistry, 2018 - Elsevier
Stability of enzymes is an important parameter for their industrial applicability. Here, we
report successful immobilization of β-amylase (bamyl) from peanut (Arachis hypogaea) onto …
report successful immobilization of β-amylase (bamyl) from peanut (Arachis hypogaea) onto …
Catalytic, thermodynamic and structural properties of an immobilized and highly thermostable alkaline protease from a haloalkaliphilic actinobacteria, Nocardiopsis …
FJ Thakrar, SP Singh - Bioresource technology, 2019 - Elsevier
A highly thermostable protease from a haloalkaliphilic actinobacteria was immobilized
employing 5 different approaches on 24 carriers. On immobilization, the activation energy …
employing 5 different approaches on 24 carriers. On immobilization, the activation energy …
Lignin from bamboo shoot shells as an activator and novel immobilizing support for α-amylase
W Gong, Z Ran, F Ye, G Zhao - Food chemistry, 2017 - Elsevier
This study examined the feasibility of α-amylase activation and immobilization, using lignin
from bamboo shoot shells (BSS). Our results demonstrated that BSS lignin is an excellent α …
from bamboo shoot shells (BSS). Our results demonstrated that BSS lignin is an excellent α …