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Immobilization of a-amylase, alkaline pectinase, and laccase enzymes onto ester-crosslinked as well as Cu-chelated cotton fabrics were carried out. Factors affecting the extent of enzyme-loading and retention activities of immobilized enzymes were studied. Proper conditions for attaining higher extent of fixation along with better retained activity were studied. The degree of antimicrobial activity of treated fabric samples against gram-negative and gram-positive bacteria, filamentous, and nonfilamentous fungi were evaluated. The antimicrobial activity is determined by the type of substrate, i.e., Cu-chelated > ester-crosslinked and activated cotton substrate, and the nature of immobilized enzyme, i.e., alkaline pectinase > a-amylase > laccase, irrespective of the used microorganism. The antimicrobial activities of the treated fabrics are completely maintained after laundering at least ten consecutive wash cycles. Further consecutive wash cycles, i.e., 20 or 30 cycles, has practically negative impact on the retained antimicrobial efficacy.

Endoglucanase (EG) from A. terreus DSM 826 grown on sugar cane bagasse as a carbon source was purified using acetone fractionation, then a Sepharose-4B chromatographic column, with purification of about 27-fold and 10.5% recovery. The optimum temperature and pH for activity of the purified EG were found to be 50 degrees C and pH 4.8, respectively. The purified enzyme can stand heating up to 50 degrees C for 1 h without apparent loss of activity. However, the enzyme, incubated at 80 degrees C for 5 min, showed about 56% loss of activity. Optimum EG activity was recorded with a citrate buffer system (pH 4.8; 0.05 M). Co2+ (2.5 x 10(-2) M) and Zn2+ (5 x 10(-2) M) were found to activate the purified EG of A. terreus DSM 826 by about 83 and 25%, respectively. On the other hand, Hg2+ inhibited the activity of the purified EG by about 50 and 71% at a concentration of 2.5 x 10(-2) and 5 x 10(-2) M, respectively. Carboxymethyl cellulose was found to be the best substrate for the purified EG, with V(max) values of 4.35 micrpmol min(-1) mg(-1) protein.

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