Robust chitinolytic activity of crab-eating monkey (Macaca fascicularis) acidic chitinase under a broad pH and temperature range

Maiko Uehara,Yukari Maruyama,Vaclav Matoska,Mikoto Okuda,Eri Tabata,Peter O Bauer,Fumitaka Oyama

doi:10.1038/s41598-021-95010-w

Abstract

Diet of the crab-eating monkey (Macaca fascicularis) consists of both plants and animals, including chitin-containing organisms such as crabs and insects. This omnivorous monkey has a high expression of acidic chitinase (CHIA) in the stomach and here, we report on its enzymatic properties under different conditions. When we compared with Mus musculus CHIA (Mm-CHIA), Macaca fascicularis CHIA (Mf-CHIA) exhibits higher chitinolytic activity at broad pH (1.0–7.0) and temperature (30–70 ℃) range. Interestingly, at its optimum pH (5.0), Mf-CHIA showed the highest activity at 65 °C while maintaining it at robust levels between 50 and 70 °C. The degradation efficiency of Mf-CHIA was superior to Mm-CHIA toward both polymeric chitin as well as an artificial chromogenic substrate. Our results show that unique features of Mf-CHIA including its thermostability warrant the nomination of this enzyme for potential agricultural and biomedical applications.

Highlights

Diet of the crab-eating monkey (Macaca fascicularis) consists of both plants and animals, including chitin-containing organisms such as crabs and insects
The recombinant Macaca fascicularis CHIA (Mf-CHIA) and Mus musculus CHIA (Mm-CHIA) enzymes were analyzed by SDS–polyacrylamide gel electrophoresis (PAGE), followed by Western blot using an anti-V5 antibody
The signal intensities of both bands were equal between Mf-CHIA and Mm-CHIA (Supplementary Fig. S3) and zymographic analysis revealed chitinolytic activity in all of them (Fig. 1c and Supplementary Fig.S4)

Summary

Introduction

Diet of the crab-eating monkey (Macaca fascicularis) consists of both plants and animals, including chitin-containing organisms such as crabs and insects. This omnivorous monkey has a high expression of acidic chitinase (CHIA) in the stomach and here, we report on its enzymatic properties under different conditions. The crab-eating monkey (Macaca fascicularis; Old World monkey) provides a crucial nonhuman primate animal model for biomedical research[26,27]. This primate’s name came from its feeding habits when different chitincontaining organisms, including crabs, comprise the central part of its d iet[28]. Common marmoset (New World monkey) CHIA is most active at pH 2.0 and degrades chitin and mealworm shells into GlcNAc dimers [(GlcNAc)2] under gastrointestinal c onditions[32]

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