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Lactase and other enzymes bound to chitin with glutaraldehyde

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TLDR
The properties of enzymes fixed on crab chitin were studied intensively and the pH optima of the fixed enzymes were shifted about one pH unit; the shift for I was toward more acid pH, for II was toward alkaline pH, and for III was toward acid pH.
Abstract
Acid tolerant lactase (I), α-chymotrypsin (II), and acid phosphatase (III) were immobilized on chitin with glutaraldehyde. Pretreatments of the chit in with acid, alkali, ammonia, and pronase were compared with respect to release of titratable amino groups and ability to retain lactase activity. Shrimp chitin appeared to be more sensitive to pretreatment conditions and so effort was concentrated on crab. An acid-alkali pretreatment was selected as most practical and economical, and the properties of enzymes fixed on crab chitin were studied intensively. The pH optima of the fixed enzymes were shifted about one pH unit; the shift for I was toward more acid pH, for II was toward alkaline pH, and for III was toward acid pH. The retained activity of immobilized I was approximately 60% that of the native enzyme. A column in continuous operation with I on chitin-glutaraldehyde gave an apparent activity half-life of 27 days.

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Effects of ultrasonic conditions and storage in acidic solutions on changes in molecular weight and polydispersity of treated chitosan

TL;DR: In this paper, the effects of ultrasonic conditions and storage in acidic solution on changes in the molecular weight and polydispersity (molecular weight distribution) of treated chitosan were explored.
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Conversion of chitinous wastes to hydrogen gas by clostridium paraputrificum M-21

TL;DR: The chitinolytic bacterium Clostridium paraputrificum strain M-21 produced 2.2 and 1.5 mol hydrogen gas from 1 mol Nacetyl-d-glucosamine (GlcNAc) and ball-milled chitin equivalent to 1 mol of Glc NAc, respectively, at pH 6.0 as discussed by the authors.
Journal ArticleDOI

Co-immobilized pectinlyase and endocellulase on chitin and Nylon supports

TL;DR: Chitin was more suitable for applications to fruit juice liquefaction because both immobilized pectinlyase and endocellulase showed higher activity at low pH and low temperature.
Journal ArticleDOI

Immobilized enzymes on chitosan columns: alpha-chymotrypsin and acid phosphatase.

TL;DR: α‐Chymotrypsin and acid phosphatase have been immobilized on chitosan, a polyaminosaccharide, without using any intermediate reagent; the immobilized enzymes are active and their activity is much higher than for chitin‐immobilized enzymes.
Journal ArticleDOI

β-Galactosidase from Aspergillus niger

TL;DR: The enzyme β-galactosidase from Aspergillus niger was purified and resolved into three multiple forms, using molecular sieving, ion-exchange, and hydrophobic chromatography, showing multiplicity was mainly due to dissimilar carbohydrate contents.
References
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Journal ArticleDOI

Preparation and measurement of the purity of the phosphatase reagent, disodium p-nitrophenyl phosphate.

TL;DR: There is presented below a simple and satisfactory method for the synthesis of the disodium salt of p-nitrophenyl phosphate and for determining its purity.
Journal ArticleDOI

A new polyamine carrier for the immobilization of proteins. Water-insoluble derivatives of pepsin and trypsin.

TL;DR: A new polymeric carrier, containing primary amino groups was prepared by coupling an ethylene maleic anhydride (1:1) copolymer (EMA), with 1.6-diaminohexane (HMD) in the presence of dicyclohexylcarbodiimide.
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