Recombinant Chlamydomonas reinhardtii chlorophyllase 1 (CrCLH1) that could catalyze chlorophyll hydrolysis to chlorophyllide and phytol in vitro was successfully expressed in Escherichia coli. The recombinant CrCLH1 was immobilized through covalent binding with a cubic (3-aminopropyl) triethoxysilane (APTES) coating on magnetic iron oxide nanoparticles (MIONPs), which led to markedly improved e...

Proteases are the most studied microbial enzymes at commercial, industrial, pharmaceutical analytical, diagnostic, effluent abatement and other sectors. An effective proteolytic enzyme producing microbial strain has been isolated from marine soil under banana tree and evaluated its extracellular protease production properties with respect to different fermentative physiological parameters. The ...

This study reports the purification and biochemical characterization of thermostable and acidic-pH-stable α-amylase from Bacillus sp. Iranian S1 isolated from the desert soil (Gandom-e-Beryan in Lut desert, Iran). Amylase production was found to be growth associated. Maximum enzyme production was in exponential phase with activity 2.93 U ml-1 at 50°C and pH 5. The enzyme was purified by isoprop...

Proteases are involved in several crucial biological processes and reported to have important physiological functions. They also have multifarious applications in different industries. The immobilized form of the enzyme further improves its industrial applicability. Here, we report covalent immobilization of a novel cysteine endopeptidase (procerain B) on amberlite MB-150 beads through glutaral...

The aim of this study was to use agro-industrial residues for the production of a halotolerant keratinolyticprotease by Actinobacterium sp. in solid-state fermentation. Among various agro-industrial residues that were evaluated, apple pomace supported maximum protease production (8400 U/g material). The optimum conditions required for enzyme production were a fermentation period of 72 h, 10% (w...

Industrial applications require enzymes highly stable and economically viable in terms of reusability. Enzyme immobilization is an exciting alternative to improve the stability of enzymatic processes. The immobilization of two commercial enzymes is reported here (cellulase and xylanase) using three chemical methods (adsorption, reticulation, and crosslinking-adsorption) and two polymeric suppor...

In this article, we describe the selection of medium components like pH, temperature, carbon sources and nitrogen sources for the optimal production of extracellular peroxidase by Coprinus sp. (AKL 02) with a series of experiments which is important for growth and enzyme production. The high quality enzyme elicited by the fungus has greater potential for industrial application especially waste ...

BACKGROUND Amylases are used in various industrial processes and a key requirement for the efficiency of these processes is the use of enzymes with high catalytic activity at ambient temperature. Unfortunately, most amylases isolated from bacteria and filamentous fungi have optimal activity above 45 °C and low pH. For example, the most commonly used industrial glucoamylases, a type of amylase t...