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Characteristics of a XIP ‐resistant xylanase from Neocallimastix sp. GMLF 1 and its advantage in barley malt saccharification
Author(s) -
Zhu Dongdong,
Liu Xinyu,
Xie Xia,
Yang Sen,
Lin Hui,
Chen Hongge
Publication year - 2020
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.14341
Subject(s) - xylanase , hydrolysis , food science , biology , xylose , fermentation , chemistry , biochemistry , enzyme
Summary The well‐studied xylanase inhibitor protein ( XIP ‐I) regularly inhibits fungi‐derived xylanases, yet some fungal xylanases are not inhibited by XIP ‐I. Based on the sequence alignment with the known XIP ‐I resistant NpXyn11A from Neocallimastix patriciarum , a new annotated xylanase from ruminal fungus Neocallimastix sp. GMLF 1 was found, noted as Xyn1B, which shared 77.8% of sequence identity with NpXyn11A and was proved to be resistant to XIP ‐I. To evaluate the performance of a XIP resistant xylanase used in barley malt saccharification, a XIP ‐I sensitive xylanase ThXyn1 from Trichoderma harzianum was chosen as a control. The barley malt saccharification experiment was carried out on the condition with or without extra XIP ‐I added. The results showed that Xyn1B displayed only slight difference in presence and absence of added XIP ‐I, with the difference of xylose released (ΔX) and the difference of mash clarity (ΔA) being 0.17 g L −1 ( P > 0.05) and 0.007 ( P > 0.05), respectively; while those for ThXyn1 group reached 0.96 g L −1 ( P < 0.01) and 0.095 ( P < 0.05), indicating that XIP ‐I did not adversely affect Xyn1B's function, but did affect ThXyn1's function. Our work for the first time suggested that a xylanase with resistance to xylanase inhibitor proteins might have an advantage in barley malt saccharification over an inhibitor sensitive xylanase.