Open AccessMethod for purification of collagen: A systematic review
Author(s) -
Nursyahidatul Azwa Awang,
Azura Amid,
Zatul Iffah Mohd Arshad
Publication year - 2020
Publication title -
asia-pacific journal of molecular biology and biotechnology/asia pacific journal of molecular biology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.137
H-Index - 19
eISSN - 2521-9839
pISSN - 0128-7451
DOI - 10.35118/apjmbb.2020.028.3.10
Subject(s) - recombinant dna , affinity chromatography , protein purification , computational biology , chemistry , biochemistry , chromatography , computer science , biology , enzyme , gene
Collagen has diverse applications in various industries and thus a various method of purifications has been developed over the years to produce high yield and high purity of collagen to fulfill collagen market demand. The objective of this qualitative systematic review is to summarize the current literature on the existing purification methods for collagen from different sources. Toward this end, three databases were searched and articles were screened for all original articles explaining the purification of collagen regardless of their main sources. After the comprehensive screening, out of 715 articles, 12 articles were chosen and were further reviewed. The analysis of the technical details, theory, advantages, and disadvantages of the techniques used are reported in this study. We found four types of purification methods that commonly used to purify various types of collagen from mammals, marine, bacteria, and recombinant collagen. The correlations between the prevalence of the method and the efficiency of collagen purification were also identified. It highlighted that many factors should be considered before choosing any method of purification such as types, sources and structure of the collagen itself. Affinity chromatography commonly used for purification of recombinant collagen as they have been genetically modified and appended by affinity tags whereas conventional purification method is preferable for non-recombinant collagen from mammalian and marine sources.