Acidic proteases from Monterey sardine (Sardinops sagax caerulea) immobilized on shrimp waste chitin and chitosan supports: searching for a by-product catalytic system

Appl Biochem Biotechnol. 2013 Oct;171(3):795-805. doi: 10.1007/s12010-013-0407-8. Epub 2013 Jul 30.

Abstract

Solid wastes generated from the seafood industry represent an important environmental pollutant; therefore, utilization of those wastes for the development of processing biochemical tools could be an attractive and clean solution for the seafood industry. This study reports the immobilization of semi-purified acidic proteases from Monterey sardine stomachs onto chitin and chitosan materials extracted from shrimp head waste. Several supports (chitosan beads, chitosan flakes, and partially deacetylated flakes) were activated either with genipin or Na-tripolyphosphate and evaluated as a mean to immobilize acidic proteases. The protein load varied within the 67-91% range on different supports. The immobilization systems based on chitosan beads achieved the highest protein loads but showed the lowest retained catalytic activities. The best catalytic behavior was obtained using partially deacetylated chitin flakes activated either with genipin or Na-tripolyphosphate. According to results, the immobilization matrix structure, as well as acetylation degree of chitin-chitosan used, has considerable influence on the catalytic behavior of immobilized proteases. Partially deacetylated chitin flakes represent a suitable option as support for enzyme immobilization because its preparation requires fewer steps than other supports. Two abundant seafood by-products were used to obtain a catalytic system with enough proteolytic activity to be considered for biotechnological applications in diverse fields.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biotechnology / methods
  • Chitin / chemistry*
  • Chitosan / chemistry
  • Enzymes, Immobilized / chemistry*
  • Enzymes, Immobilized / isolation & purification
  • Fishes / metabolism
  • Industrial Waste*
  • Iridoids / pharmacology
  • Penaeidae / chemistry*
  • Penaeidae / drug effects
  • Peptide Hydrolases / chemistry*
  • Peptide Hydrolases / isolation & purification
  • Polyphosphates / pharmacology

Substances

  • Enzymes, Immobilized
  • Industrial Waste
  • Iridoids
  • Polyphosphates
  • Chitin
  • Chitosan
  • genipin
  • Peptide Hydrolases
  • triphosphoric acid